# genes

id: YPR188C
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","genes_by_uniquename":{"SJAG_01665":null,"YPR188C":null},"has_protein_features":false,"name":"MLC2","ortholog_annotations":[{"gene_uniquename":"YPR188C","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_01665","reference_uniquename":"PMID:29761456"}],"product":"Regulatory light chain for the type II myosin Myo1p; binds to an IQ motif of Myo1p, localization to the bud neck depends on Myo1p; involved in the disassembly of the Myo1p ring","references_by_uniquename":{"PMID:29761456":null},"secondary_identifier":"SGD:S000006392","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR188C"}


id: YPR189W
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","genes_by_uniquename":{"SJAG_03805":null,"YPR189W":null},"has_protein_features":false,"name":"SKI3","ortholog_annotations":[{"gene_uniquename":"YPR189W","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_03805","reference_uniquename":"PMID:29761456"}],"product":"Ski complex component and TPR protein; mediates 3'-5' RNA degradation by the cytoplasmic exosome; null mutants have superkiller phenotype of increased viral dsRNAs and are synthetic lethal with mutations in 5'-3' mRNA decay; mutations in the human ortholog, TTC37, causes Syndromic diarrhea/Trichohepatoenteric (SD/THE) syndrome","references_by_uniquename":{"PMID:29761456":null},"secondary_identifier":"SGD:S000006393","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR189W"}


id: YPR190C
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","genes_by_uniquename":{"SJAG_00619":null,"YPR190C":null},"has_protein_features":false,"name":"RPC82","ortholog_annotations":[{"gene_uniquename":"YPR190C","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_00619","reference_uniquename":"PMID:29761456"}],"product":"RNA polymerase III subunit C82","references_by_uniquename":{"PMID:29761456":null},"secondary_identifier":"SGD:S000006394","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR190C"}


id: YPR191W
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","genes_by_uniquename":{"SJAG_00755":null,"YPR191W":null},"has_protein_features":false,"name":"QCR2","ortholog_annotations":[{"gene_uniquename":"YPR191W","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_00755","reference_uniquename":"PMID:29761456"}],"product":"Subunit 2 of ubiquinol cytochrome-c reductase (Complex III); Complex III is a component of the mitochondrial inner membrane electron transport chain; phosphorylated; transcription is regulated by Hap1p, Hap2p/Hap3p, and heme","references_by_uniquename":{"PMID:29761456":null},"secondary_identifier":"SGD:S000006395","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR191W"}


id: YPR192W
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","has_protein_features":false,"name":"AQY1","product":"Spore-specific water channel; mediates the transport of water across cell membranes, developmentally controlled; may play a role in spore maturation, probably by allowing water outflow, may be involved in freeze tolerance","secondary_identifier":"SGD:S000006396","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR192W"}


id: YPR193C
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","genes_by_uniquename":{"SJAG_03288":null,"YPR193C":null},"has_protein_features":false,"name":"HPA2","ortholog_annotations":[{"gene_uniquename":"YPR193C","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_03288","reference_uniquename":"PMID:29761456"}],"product":"Tetrameric histone acetyltransferase; has similarity to Gcn5p, Hat1p, Elp3p, and Hpa3p; acetylates histones H3 and H4 in vitro and exhibits autoacetylation activity; also acetylates polyamines","references_by_uniquename":{"PMID:29761456":null},"secondary_identifier":"SGD:S000006397","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR193C"}


id: YPR194C
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","genes_by_uniquename":{"SJAG_00922":null,"SJAG_01660":null,"YPR194C":null},"has_protein_features":false,"name":"OPT2","ortholog_annotations":[{"gene_uniquename":"YPR194C","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_00922","reference_uniquename":"PMID:29761456"},{"gene_uniquename":"YPR194C","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_01660","reference_uniquename":"PMID:29761456"}],"product":"Oligopeptide transporter; localized to peroxisomes and affects glutathione redox homeostasis; also localizes to the plasma membrane (PM) and to the late Golgi, and has a role in maintenance of lipid asymmetry between the inner and outer leaflets of the PM; member of the OPT family, with potential orthologs in S. pombe and C. albicans; also plays a role in formation of mature vacuoles and in polarized cell growth","references_by_uniquename":{"PMID:29761456":null},"secondary_identifier":"SGD:S000006398","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR194C"}


id: YPR195C
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","has_protein_features":false,"product":"Putative protein of unknown function; conserved across S. cerevisiae strains","secondary_identifier":"SGD:S000006399","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR195C"}


id: YPR196W
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","has_protein_features":false,"product":"Putative maltose-responsive transcription factor","secondary_identifier":"SGD:S000006400","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR196W"}


id: YPR197C
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","has_protein_features":false,"product":"Dubious open reading frame; unlikely to encode a functional protein, based on available experimental and comparative sequence data; overlaps ORF SGE1/YPR198W","secondary_identifier":"SGD:S000006401","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR197C"}


id: YPR198W
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","genes_by_uniquename":{"SJAG_01336":null,"SJAG_01636":null,"SJAG_01923":null,"SJAG_04715":null,"SJAG_04983":null,"YPR198W":null},"has_protein_features":false,"name":"SGE1","ortholog_annotations":[{"gene_uniquename":"YPR198W","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_01336","reference_uniquename":"PMID:29761456"},{"gene_uniquename":"YPR198W","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_01636","reference_uniquename":"PMID:29761456"},{"gene_uniquename":"YPR198W","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_01923","reference_uniquename":"PMID:29761456"},{"gene_uniquename":"YPR198W","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_04715","reference_uniquename":"PMID:29761456"},{"gene_uniquename":"YPR198W","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_04983","reference_uniquename":"PMID:29761456"}],"product":"Plasma membrane multidrug transporter; member of the major facilitator superfamily; acts as an extrusion permease; partial multicopy suppressor of gal11 mutations","references_by_uniquename":{"PMID:29761456":null},"secondary_identifier":"SGD:S000006402","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR198W"}


id: YPR199C
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","has_protein_features":false,"name":"ARR1","product":"Transcriptional activator of the basic leucine zipper (bZIP) family; required for transcription of genes involved in resistance to arsenic compounds; directly binds trivalent arsenic (As(III)) as does K. lactis ortholog, KIYAP8","secondary_identifier":"SGD:S000006403","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR199C"}


id: YPR200C
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","genes_by_uniquename":{"SJAG_04166":null,"YPR200C":null},"has_protein_features":false,"name":"ARR2","ortholog_annotations":[{"gene_uniquename":"YPR200C","ortholog_taxonid":4897,"ortholog_uniquename":"SJAG_04166","reference_uniquename":"PMID:29761456"}],"product":"Arsenate reductase required for arsenate resistance; converts arsenate to arsenite which can then be exported from cells by Arr3p","references_by_uniquename":{"PMID:29761456":null},"secondary_identifier":"SGD:S000006404","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR200C"}


id: YPR201W
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","has_protein_features":false,"name":"ARR3","product":"Plasma membrane metalloid/H+ antiporter; member of bile/arsenite/riboflavin transporter (BART) superfamily; transports arsenite and antimonite; required for resistance to arsenic compounds; transcription is activated by Arr1p in the presence of arsenite; protein displays 10 transmembrane segments with cytoplasmically oriented N- and C-terminal domains","secondary_identifier":"SGD:S000006405","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR201W"}


id: YPR202W
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","has_protein_features":false,"product":"Putative protein of unknown function; similar to telomere-encoded helicases; down-regulated at low calcium levels; YPR202W is not an essential gene; transcript is predicted to be spliced but there is no evidence that it is spliced in vivo","secondary_identifier":"SGD:S000006406","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR202W"}


id: YPR203W
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","has_protein_features":false,"product":"Putative protein of unknown function","secondary_identifier":"SGD:S000006407","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR203W"}


id: YPR204C-A
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","has_protein_features":false,"product":"Protein of unknown function; identified by gene-trapping, microarray-based expression analysis, and genome-wide homology searching","secondary_identifier":"SGD:S000028727","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR204C-A"}


id: YPR204W
data:
  {"cv_annotations":{},"deletion_viability":"unknown","feature_so_termid":"SO:0000704","feature_type":"gene","has_protein_features":false,"product":"DNA helicase encoded within the telomeric Y' element; Y' -helicase protein 1","secondary_identifier":"SGD:S000006408","taxonid":4932,"taxonomic_distribution":"not curated","transcript_so_termid":null,"uniquename":"YPR204W"}


# refs

id: PMID:33791858
data:
  {"abstract":"Mitogen-activated protein kinase (MAPK) signalling pathways regulate multiple cellular functions in eukaryotic organisms in response to environmental cues, including the dynamic remodeling of the actin cytoskeleton. The fission yeast S. pombe is an optimal model to investigate the conserved regulatory mechanisms of cytokinesis, which relies in an actomyosin-based contractile ring (CAR) that prompts the physical separation of daughter cells during cellular division. Our group has recently shown that p38 MAPK ortholog Sty1, the core component of the stress-activated pathway (SAPK), negatively modulates CAR assembly and integrity in S. pombe during actin cytoskeletal damage induced with Latrunculin A and in response to environmental stress. This response involves downregulation of protein levels of the formin For3, which assembles actin filaments for cables and the CAR, likely through an ubiquitin-mediated degradation mechanism. Contrariwise, Sty1 function positively reinforces CAR assembly during stress in the close relative dimorphic fission yeast S. japonicus. The opposite effect of SAPK signaling on CAR integrity may represent an evolutionary refined adaptation to cope with the marked differences in cytokinesis onset in both fission yeast species.","alleles_by_uniquename":{"SJAG_00266:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00266","name":"atf1delta","uniquename":"SJAG_00266:allele-1"},"SJAG_02592:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02592","name":"sty1delta","uniquename":"SJAG_02592:allele-1"}},"annotation_curators":[{"annotation_count":4,"community_curator":true,"file_name":null,"file_type":null,"name":"Elisa Gómez Gil","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-09-14","authors":"Madrid M, Gómez-Gil E, Cansado J","authors_abbrev":"Madrid M et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-09-14 21:24:28","canto_curator_name":"Elisa Gómez Gil","canto_curator_role":"community","canto_first_approved_date":"2021-09-14 21:24:28","canto_session_key":"84ac20b0ff20a3cd","canto_session_submitted_date":"2021-09-14 16:45:32","canto_triage_status":"Curatable","citation":"Curr Genet 2021 Oct;67(5):715-721","cv_annotations":{"PSI-MOD":[{"annotations":[114508],"is_not":false,"summary":null,"term":"MOD:00696"}],"single_locus_phenotype":[{"annotations":[114507],"is_not":false,"summary":null,"term":"FYPO:0002998"},{"annotations":[114505,114506],"is_not":false,"summary":null,"term":"FYPO:0000107"}]},"doi":"10.1007/s00294-021-01155-6","gene_count":2,"genes_by_uniquename":{"SJAG_00266":null,"SJAG_02592":null},"genotypes_by_uniquename":{"atf1delta":{"display_name":"atf1delta","display_uniquename":"atf1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00266:allele-1","expression":"Null"}]}]},"sty1delta":{"display_name":"sty1delta","display_uniquename":"sty1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02592:allele-1","expression":"Null"}]}]}},"ltp_gene_count":2,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-04-01","pubmed_publication_date":"Oct 2021","terms_by_termid":{"FYECO:0000248":null,"FYPO:0000107":null,"FYPO:0002998":null,"FYPO_EXT:0000001":null,"GO:0120306":null,"MOD:00696":null},"title":"Negative control of cytokinesis by stress-activated MAPK signaling.","uniquename":"PMID:33791858"}


id: PMID:7214237
data:
  {"abstract":"Hybridization studies based on the prototrophic selection technique, involving the use of auxotrophic mutants of strains of five accepted species of the genus Schizosaccharomyces, are reported. Intrastrain recombinants were recovered in five out of six tested parental pairs. Interstrain recombinants were recovered from crosses involving strains of S. japonicus and strains of S. pombe. No recombinants were recovered in 62 interspecific crosses involving all possible combinations of the six representatives of the genus.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Johannsen E","authors_abbrev":"Johannsen E","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Can J Microbiol 1981 Feb;27(2):184-91","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1981","pubmed_entrez_date":"1981-02-01","pubmed_publication_date":"Feb 1981","terms_by_termid":{},"title":"Hybridization studies within the genus Schizosaccharomyces Lindner.","uniquename":"PMID:7214237"}


id: PMID:25942548
data:
  {"abstract":"New work shows the anillin-related protein Mid1 does not position the cytokinetic ring in the fission yeast Schizosaccharomyces japonicus, unlike its role in S. pombe. Further analysis suggests the conserved function of Mid1-like anillin proteins may be in scaffolding, not positioning, the cytokinetic ring. ","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Moseley JB","authors_abbrev":"Moseley JB","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Curr Biol 2015 May 04;25(9):R364-6","cv_annotations":{},"doi":"10.1016/j.cub.2015.03.017","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2015","pubmed_entrez_date":"2015-05-06","pubmed_publication_date":"04 May 2015","terms_by_termid":{},"title":"Cytokinesis: does Mid1 have an identity crisis?","uniquename":"PMID:25942548"}


id: PMID:34656184
data:
  {"abstract":"In most fungi, quinone-dependent Class-II dihydroorotate dehydrogenases (DHODs) are essential for pyrimidine biosynthesis. Coupling of these Class-II DHODHs to mitochondrial respiration makes their in vivo activity dependent on oxygen availability. Saccharomyces cerevisiae and closely related yeast species harbor a cytosolic Class-I DHOD (Ura1) that uses fumarate as electron acceptor and thereby enables anaerobic pyrimidine synthesis. Here, we investigate DHODs from three fungi (the Neocallimastigomycete Anaeromyces robustus and the yeasts Schizosaccharomyces japonicus and Dekkera bruxellensis) that can grow anaerobically but, based on genome analysis, only harbor a Class-II DHOD.\nHeterologous expression of putative Class-II DHOD-encoding genes from fungi capable of anaerobic, pyrimidine-prototrophic growth (Arura9, SjURA9, DbURA9) in an S. cerevisiae ura1Δ strain supported aerobic as well as anaerobic pyrimidine prototrophy. A strain expressing DbURA9 showed delayed anaerobic growth without pyrimidine supplementation. Adapted faster growing DbURA9-expressing strains showed mutations in FUM1, which encodes fumarase. GFP-tagged SjUra9 and DbUra9 were localized to S. cerevisiae mitochondria, while ArUra9, whose sequence lacked a mitochondrial targeting sequence, was localized to the yeast cytosol. Experiments with cell extracts showed that ArUra9 used free FAD and FMN as electron acceptors. Expression of SjURA9 in S. cerevisiae reproducibly led to loss of respiratory competence and mitochondrial DNA. A cysteine residue (C265 in SjUra9) in the active sites of all three anaerobically active Ura9 orthologs was shown to be essential for anaerobic activity of SjUra9 but not of ArUra9.\nActivity of fungal Class-II DHODs was long thought to be dependent on an active respiratory chain, which in most fungi requires the presence of oxygen. By heterologous expression experiments in S. cerevisiae, this study shows that phylogenetically distant fungi independently evolved Class-II dihydroorotate dehydrogenases that enable anaerobic pyrimidine biosynthesis. Further structure-function studies are required to understand the mechanistic basis for the anaerobic activity of Class-II DHODs and an observed loss of respiratory competence in S. cerevisiae strains expressing an anaerobically active DHOD from Sch. japonicus.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Bouwknegt J, Koster CC, Vos AM, Ortiz-Merino RA, Wassink M, Luttik MAH, van den Broek M, Hagedoorn PL, Pronk JT","authors_abbrev":"Bouwknegt J et al.","canto_added_date":"2023-05-04 00:40:04","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Fungal Biol Biotechnol 2021 Oct 16;8(1):10","cv_annotations":{},"doi":"10.1186/s40694-021-00117-4","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-10-17","pubmed_publication_date":"16 Oct 2021","terms_by_termid":{},"title":"Class-II dihydroorotate dehydrogenases from three phylogenetically distant fungi support anaerobic pyrimidine biosynthesis.","uniquename":"PMID:34656184"}


id: PMID:37164017
data:
  {"abstract":"Most eukaryotes respire oxygen, using it to generate biomass and energy. However, a few organisms have lost the capacity to respire. Understanding how they manage biomass and energy production may illuminate the critical points at which respiration feeds into central carbon metabolism and explain possible routes to its optimization. Here, we use two related fission yeasts, Schizosaccharomyces pombe and Schizosaccharomyces japonicus, as a comparative model system. We show that although S. japonicus does not respire oxygen, unlike S. pombe, it is capable of efficient NADH oxidation, amino acid synthesis, and ATP generation. We probe possible optimization strategies through the use of stable isotope tracing metabolomics, mass isotopologue distribution analysis, genetics, and physiological experiments. S. japonicus appears to have optimized cytosolic NADH oxidation via glycerol-3-phosphate synthesis. It runs a fully bifurcated TCA pathway, sustaining amino acid production. Finally, we propose that it has optimized glycolysis to maintain high ATP/ADP ratio, in part by using the pentose phosphate pathway as a glycolytic shunt, reducing allosteric inhibition of glycolysis and supporting biomass generation. By comparing two related organisms with vastly different metabolic strategies, our work highlights the versatility and plasticity of central carbon metabolism in eukaryotes, illuminating critical adaptations supporting the preferential use of glycolysis over oxidative phosphorylation.","alleles_by_uniquename":{"SJAG_00409:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00409","name":"gpd1delta","uniquename":"SJAG_00409:allele-1"},"SJAG_00601:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00601","name":"rip1delta","uniquename":"SJAG_00601:allele-1"},"SJAG_01355:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01355","name":"cox6delta","uniquename":"SJAG_01355:allele-1"},"SJAG_01753:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01753","name":"mdh1delta","uniquename":"SJAG_01753:allele-1"},"SJAG_02796:allele-1":{"allele_type":"amino_acid_mutation","description":"A343T","gene_uniquename":"SJAG_02796","name":"pyk1-A343T","uniquename":"SJAG_02796:allele-1"},"SJAG_03920:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03920","name":"sdh3delta","uniquename":"SJAG_03920:allele-1"},"SJAG_04843:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04843","name":"fum1delta","uniquename":"SJAG_04843:allele-1"}},"annotation_curators":[{"annotation_count":20,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2023-05-18","authors":"Alam S, Gu Y, Reichert P, Bähler J, Oliferenko S","authors_abbrev":"Alam S et al.","canto_added_date":"2023-05-12 00:40:04","canto_annotation_status":"APPROVED","canto_approved_date":"2023-05-18 12:11:55","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2023-05-18 12:11:54","canto_session_key":"94bcbfb72cf94809","canto_session_submitted_date":"2023-05-18 12:11:43","canto_triage_status":"Curatable","citation":"Curr Biol 2023 Apr 30;","cv_annotations":{"single_locus_phenotype":[{"annotations":[114524],"is_not":false,"summary":null,"term":"FYPO:0007363"},{"annotations":[114522],"is_not":false,"summary":null,"term":"FYPO:0000026"},{"annotations":[114521],"is_not":false,"summary":null,"term":"FYPO:0001355"},{"annotations":[114523],"is_not":false,"summary":null,"term":"FYPO:0001489"},{"annotations":[114525],"is_not":false,"summary":null,"term":"FYPO:0004165"},{"annotations":[114519,114520],"is_not":false,"summary":null,"term":"FYPO:0007790"},{"annotations":[114513,114516],"is_not":false,"summary":null,"term":"FYPO:0000760"},{"annotations":[114515,114518],"is_not":false,"summary":null,"term":"FYPO:0000579"},{"annotations":[114514,114517],"is_not":false,"summary":null,"term":"FYPO:0000590"},{"annotations":[114510,114511,114512],"is_not":false,"summary":null,"term":"FYPO:0001357"},{"annotations":[114509],"is_not":false,"summary":null,"term":"FYPO:0001234"},{"annotations":[114526,114527,114528],"is_not":false,"summary":null,"term":"FYPO:0002058"}]},"doi":"10.1016/j.cub.2023.04.046","gene_count":7,"genes_by_uniquename":{"SJAG_00409":null,"SJAG_00601":null,"SJAG_01355":null,"SJAG_01753":null,"SJAG_02796":null,"SJAG_03920":null,"SJAG_04843":null},"genotypes_by_uniquename":{"cox6delta":{"display_name":"cox6delta","display_uniquename":"cox6delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01355:allele-1","expression":"Null"}]}]},"fum1delta":{"display_name":"fum1delta","display_uniquename":"fum1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04843:allele-1","expression":"Null"}]}]},"gpd1delta":{"display_name":"gpd1delta","display_uniquename":"gpd1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00409:allele-1","expression":"Null"}]}]},"mdh1delta":{"display_name":"mdh1delta","display_uniquename":"mdh1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01753:allele-1","expression":"Null"}]}]},"pyk1-A343T-A343T-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"pyk1-A343T(aa)","display_uniquename":"pyk1-A343T-A343T-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02796:allele-1","expression":"Not assayed or wild type"}]}]},"rip1delta":{"display_name":"rip1delta","display_uniquename":"rip1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00601:allele-1","expression":"Null"}]}]},"sdh3delta":{"display_name":"sdh3delta","display_uniquename":"sdh3delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03920:allele-1","expression":"Null"}]}]}},"ltp_gene_count":7,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2023","pubmed_entrez_date":"2023-05-10","pubmed_publication_date":"30 Apr 2023","terms_by_termid":{"FYECO:0000005":null,"FYECO:0000015":null,"FYECO:0000126":null,"FYECO:0000137":null,"FYPO:0000026":null,"FYPO:0000579":null,"FYPO:0000590":null,"FYPO:0000760":null,"FYPO:0001234":null,"FYPO:0001355":null,"FYPO:0001357":null,"FYPO:0001489":null,"FYPO:0002058":null,"FYPO:0004165":null,"FYPO:0007363":null,"FYPO:0007790":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"FYPO_EXT:0000003":null},"title":"Optimization of energy production and central carbon metabolism in a non-respiring eukaryote.","uniquename":"PMID:37164017"}


id: PMID:2197287
data:
  {"abstract":"Changes in the distribution of microtubules and F-actin through the cell division cycle of the fission yeast Schizosaccharomyces japonicus var. versatilis were investigated by fluorescence microscopy. The fluorescence images obtained with S. japonicus were markedly superior to those previously reported for S. pombe and revealed new details of cytoskeletal organization in this important genus. As in S. pombe, F-actin in S. japonicus was present as a concentration of 'dots' at the growing poles of interphase cells and as a filamentous equatorial ring directing the deposition of the cytokinetic septum. The transition between these two states occurred at late anaphase, in contrast to the situation in S. pombe where the appearance of the equatorial actin ring is tightly coupled to the early events of mitosis. During the course of cytokinesis in S. japonicus the actin ring constricted and broadened, suggesting that it is contractile. Microtubule organization in S. japonicus also revealed interesting differences from S. pombe. Whereas in S. pombe cytoplasmic microtubules are reinitiated from a pair of microtubule organizing centres (MTOCs) at the cell equator, in S. japonicus they arise by extensive microtubule growth from the spindle poles. Western blots of cell extracts enriched for tubulin by DEAE-Sephadex chromatography showed that, like S. pombe, S. japonicus contains two alpha-tubulins and a single beta-tubulin. Whilst the alpha 1- and beta-tubulins from the two species comigrated on one-dimensional polyacrylamide gels, the alpha 2 species were electrophoretically distinct. Although fundamental differences clearly exist between the two species, S. japonicus could prove to be a useful tool in basic studies of fission yeast cell biology.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Alfa CE, Hyams JS","authors_abbrev":"Alfa CE et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"J Cell Sci 1990 May;96 ( Pt 1):71-7","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1990","pubmed_entrez_date":"1990-05-01","pubmed_publication_date":"May 1990","terms_by_termid":{},"title":"Distribution of tubulin and actin through the cell division cycle of the fission yeast Schizosaccharomyces japonicus var. versatilis: a comparison with Schizosaccharomyces pombe.","uniquename":"PMID:2197287"}


id: PMID:30726171
data:
  {"abstract":"Many fungal species are dimorphic, exhibiting both unicellular yeast-like and filamentous forms. Schizosaccharomyces japonicus, a member of the fission yeast clade, is one such dimorphic fungus. Here, we first identify fruit extracts as natural, stress-free, starvation-independent inducers of filamentation, which we use to describe the properties of the dimorphic switch. During the yeast-to-hypha transition, the cell evolves from a bipolar to a unipolar system with 10-fold accelerated polarized growth but constant width, vacuoles segregated to the nongrowing half of the cell, and hyper-lengthening of the cell. We demonstrate unusual features of S. japonicus hyphae: these cells lack a Spitzenkörper, a vesicle distribution center at the hyphal tip, but display more rapid cytoskeleton-based transport than the yeast form, with actin cables being essential for the transition. S. japonicus hyphae also remain mononuclear and undergo complete cell divisions, which are highly asymmetric: one daughter cell inherits the vacuole, the other the growing tip. We show that these elongated cells scale their nuclear size, spindle length, and elongation rates, but display altered division size controls. This establishes S. japonicus as a unique system that switches between symmetric and asymmetric modes of growth and division.","alleles_by_uniquename":{"SJAG_02392:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02392","name":"pom1delta","uniquename":"SJAG_02392:allele-1"},"SJAG_02695:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02695","name":"tip1delta","uniquename":"SJAG_02695:allele-1"},"SJAG_04703:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04703","name":"for3delta","uniquename":"SJAG_04703:allele-1"}},"annotation_curators":[{"annotation_count":21,"community_curator":true,"file_name":null,"file_type":null,"name":"Sophie Martin","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-06-16","authors":"Kinnaer C, Dudin O, Martin SG","authors_abbrev":"Kinnaer C et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-06-16 18:49:31","canto_curator_name":"Sophie Martin","canto_curator_role":"community","canto_first_approved_date":"2021-06-16 18:49:31","canto_session_key":"bf05a60cb09b4cdb","canto_session_submitted_date":"2021-06-04 10:25:08","canto_triage_status":"Curatable","citation":"Mol Biol Cell 2019 04 01;30(8):975-991","cv_annotations":{"cellular_component":[{"annotations":[114416],"is_not":false,"summary":null,"term":"GO:0051286"},{"annotations":[114398,114400,114402,114404,114406,114408],"is_not":false,"summary":null,"term":"GO:0035838"},{"annotations":[114417],"is_not":false,"summary":null,"term":"GO:0085039"},{"annotations":[114399,114401,114403,114405,114407,114409],"is_not":false,"summary":null,"term":"GO:0001411"},{"annotations":[114410],"is_not":false,"summary":null,"term":"GO:0035371"},{"annotations":[114411],"is_not":false,"summary":null,"term":"GO:0030133"}],"single_locus_phenotype":[{"annotations":[114413],"is_not":false,"summary":null,"term":"FYPO:0003315"},{"annotations":[114414],"is_not":false,"summary":null,"term":"FYPO:0001355"},{"annotations":[114418],"is_not":false,"summary":null,"term":"FYPO:0007801"},{"annotations":[114415],"is_not":false,"summary":null,"term":"FYPO:0004293"},{"annotations":[114412],"is_not":false,"summary":null,"term":"FYPO:0001956"}]},"doi":"10.1091/mbc.E18-12-0774","gene_count":9,"genes_by_uniquename":{"SJAG_01196":null,"SJAG_02392":null,"SJAG_02695":null,"SJAG_03011":null,"SJAG_03625":null,"SJAG_03915":null,"SJAG_04624":null,"SJAG_04703":null,"SJAG_04960":null},"genotypes_by_uniquename":{"for3delta":{"display_name":"for3delta","display_uniquename":"for3delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04703:allele-1","expression":"Null"}]}]},"pom1delta":{"display_name":"pom1delta","display_uniquename":"pom1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02392:allele-1","expression":"Null"}]}]},"tip1delta":{"display_name":"tip1delta","display_uniquename":"tip1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02695:allele-1","expression":"Null"}]}]}},"ltp_gene_count":9,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2019","pubmed_entrez_date":"2019-02-07","pubmed_publication_date":"01 04 2019","terms_by_termid":{"FYPO:0001355":null,"FYPO:0001956":null,"FYPO:0003315":null,"FYPO:0004293":null,"FYPO:0007801":null,"GO:0001411":null,"GO:0030133":null,"GO:0035371":null,"GO:0035838":null,"GO:0051286":null,"GO:0085039":null},"title":"Yeast-to-hypha transition of Schizosaccharomyces japonicus in response to environmental stimuli.","uniquename":"PMID:30726171"}


id: PMID:7612397
data:
  {"abstract":"The ultrastructure of isolated cell walls of Schizosaccharomyces pombe was studied by electron microscopy after treatment with the following purified enzymes: endo-beta-(1-->3)-glucanase, endo-beta-(-->6)-glucanase, and endo-alpha-(1-->3)-glucanase produced by Bacillus circulans; exo-beta-(1-->3)-glucanase and endo-beta-(1-->3)-glucanase produced by Schizosaccharomyces japonicus var. versatilis. The exo-beta-(1-->3)-glucanase had no detectable effect on the walls, but amorphous wall material was removed by action of the endo-beta-(1-->3)- and endo-beta-(1-->6)-glucanases of B. circulans to reveal a wall component consisting of densely interwoven microfibrils. The fibrils were hydrolyzed by treatment with the Schiz. japonicus endo-beta-(1-->3)-glucanase followed by B. circulans endo-alpha-(1-->3)-glucanase--suggesting that they were composed of -beta-(1-->3)-linked glucan and alpha-(1-->3)-linked glucan. The presence of a fibrillar component in untreated walls was evident after negative staining.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Kopecká M, Fleet GH, Phaff HJ","authors_abbrev":"Kopecká M et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"J Struct Biol 1995 Mar;114(2):140-52","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1995","pubmed_entrez_date":"1995-03-01","pubmed_publication_date":"Mar 1995","terms_by_termid":{},"title":"Ultrastructure of the cell wall of Schizosaccharomyces pombe following treatment with various glucanases.","uniquename":"PMID:7612397"}


id: PMID:37233261
data:
  {"abstract":"Gene targeting is a commonly used method to reveal the function of genes. Although it is an attractive tool for molecular studies, it can frequently be a challenge because its efficiency can be low and it requires the screening of a large number of transformants. Generally, these problems originate from the elevated level of ectopic integration caused by non-homologous DNA end joining (NHEJ). To eliminate this problem, NHEJ-related genes are frequently deleted or disrupted. Although these manipulations can improve gene targeting, the phenotype of the mutant strains raised the question of whether mutations have side effects. The aim of this study was to disrupt the  lig4  gene in the dimorphic fission yeast,  S. japonicus , and investigate the phenotypic changes of the mutant strain. The mutant cells have shown various phenotypic changes, such as increased sporulation on complete medium, decreased hyphal growth, faster chronological aging, and higher sensitivity to heat shock, UV light, and caffeine. In addition, higher flocculation capacity has been observed, especially at lower sugar concentrations. These changes were supported by transcriptional profiling. Many genes belonging to metabolic and transport processes, cell division, or signaling had altered mRNA levels compared to the control strain. Although the disruption improved the gene targeting, we assume that the  lig4  inactivation can cause unexpected physiological side effects, and we have to be very careful with the manipulations of the NHEJ-related genes. To reveal the exact mechanisms behind these changes, further investigations are required.","alleles_by_uniquename":{"SJAG_02527:allele-1":{"allele_type":"disruption","description":"RNA sequencing revealed that only the 5' end of the disrupted allele showed low RNA expression and coverage","gene_uniquename":"SJAG_02527","name":"lig4::KanMX6","uniquename":"SJAG_02527:allele-1"}},"annotation_curators":[{"annotation_count":7,"community_curator":true,"file_name":null,"file_type":null,"name":"Ida Miklos","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2023-08-08","authors":"Acs-Szabo L, Papp LA, Takacs S, Miklos I","authors_abbrev":"Acs-Szabo L et al.","canto_added_date":"2023-05-27 00:40:04","canto_annotation_status":"APPROVED","canto_approved_date":"2023-08-08 20:07:33","canto_curator_name":"Ida Miklos","canto_curator_role":"community","canto_first_approved_date":"2023-08-08 20:07:33","canto_session_key":"c74bdd0a67b132f8","canto_session_submitted_date":"2023-08-08 20:07:15","canto_triage_status":"Curatable","citation":"J Fungi (Basel) 2023 May 10;9(5)","cv_annotations":{"single_locus_phenotype":[{"annotations":[114499],"is_not":false,"summary":null,"term":"FYPO:0007776"},{"annotations":[114501],"is_not":false,"summary":null,"term":"FYPO:0009111"},{"annotations":[114498],"is_not":false,"summary":null,"term":"FYPO:0000588"},{"annotations":[114504],"is_not":false,"summary":null,"term":"FYPO:0005705"},{"annotations":[114502],"is_not":false,"summary":null,"term":"FYPO:0005231"},{"annotations":[114500],"is_not":false,"summary":null,"term":"FYPO:0000097"},{"annotations":[114503],"is_not":false,"summary":null,"term":"FYPO:0001408"}]},"doi":"10.3390/jof9050550","gene_count":1,"genes_by_uniquename":{"SJAG_02527":null},"genotypes_by_uniquename":{"lig4::KanMX6-RNA_sequencing_revealed_that_only_the_5'_end_of_the_disrupted_allele_showed_low_RNA_expression_and_coverage-disruption-expression-knockdown":{"display_name":"lig4::KanMX6(RNA sequencing revealed that only the 5' end of the disrupted allele showed low RNA expression and coverage)[Knockdown]","display_uniquename":"lig4::KanMX6-RNA_sequencing_revealed_that_only_the_5'_end_of_the_disrupted_allele_showed_low_RNA_expression_and_coverage-disruption-expression-knockdown","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02527:allele-1","expression":"Knockdown"}]}]}},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2023","pubmed_entrez_date":"2023-05-26","pubmed_publication_date":"10 May 2023","terms_by_termid":{"FYECO:0000005":null,"FYECO:0000081":null,"FYECO:0000117":null,"FYECO:0000126":null,"FYECO:0000137":null,"FYECO:0000315":null,"FYPO:0000097":null,"FYPO:0000588":null,"FYPO:0001408":null,"FYPO:0005231":null,"FYPO:0005705":null,"FYPO:0007776":null,"FYPO:0009111":null},"title":"Disruption of the  Schizosaccharomyces japonicus lig4  Disturbs Several Cellular Processes and Leads to a Pleiotropic Phenotype.","uniquename":"PMID:37233261"}


id: PMID:31732056
data:
  {"abstract":"Vitis davidii Föex is widely planted in South China as a potential wine making grape. In this study, yeast communities during the spontaneous fermentations of two varieties of Vitis davidii Föex in Guizhou, China were investigated. Hanseniaspora uvarum, Pichia terricola, Saccharomyces cerevisiae/S. mikatae, and Schizosaccharomyces japonicus were the four main yeast species detected by culture-dependent and high-throughput sequencing approaches. However, the composition of minor yeast species was quite different as revealed by the two approaches. Ten yeast species including Debaryomyces hansenii, Rhodotorula mucilaginosa, Sporidiobolus paraoseus, Starmerella bacillaris, Zygoascus meyerae, etc. were detected by culture-dependent approaches, whereas the other five species were found by high-throughput sequencing analysis. S. japonicus was widely found during spontaneous fermentations and its concentrations were mostly higher than that of S. cerevisiae. The difference in grape varieties and fermentation conditions contributed to yeast diversity. The results of this study provide basic information on indigenous yeast diversity from Vitis davidii Föex in Guizhou, which would help to exploit the potential of non-Saccharomyces yeast species with good oenological attributes.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Wang C, Wu C, Qiu S","authors_abbrev":"Wang C et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Biotech","citation":"Food Res Int 2019 12;126:108582","cv_annotations":{},"doi":"10.1016/j.foodres.2019.108582","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2019","pubmed_entrez_date":"2019-11-17","pubmed_publication_date":"12 2019","terms_by_termid":{},"title":"Yeast diversity investigation of Vitis davidii Föex during spontaneous fermentations using culture-dependent and high-throughput sequencing approaches.","uniquename":"PMID:31732056"}


id: PMID:9720056
data:
  {"abstract":"The cells of Schizosaccharomyces japonicus var. versatilis responded to the presence of cytochalasin D (CD), an inhibitor of actin polymerization, by the disappearance of contractile actin rings (ARs) that had already formed and by inhibition of new ring formation. Actin cables disappeared. Actin patches remained preserved and became co-localized with regions of actual cell wall formation (at cell poles and at the site of septum development). Removal of the AR arrested formation of the primary septum and led to the production of aberrant septum protrusions in that region. Nuclear division was accomplished in the presence of CD but new ARs were not produced. The wall (septum) material was deposited in the form of a wide band at the inner surface of the lateral cell wall in the cell centre. This layer showed a thin fibrillar structure. The removal of CD resulted in rapid formation of new ARs in the equatorial region of the cells. This implies that the signal for AR localization was not abolished either by CD effects or by removal of an AR already formed. Some of the newly developed ARs showed atypical localization and orientation. In addition, redundant, subcortically situated actin bundles were produced. The removal of CD was quickly followed by the development of primary septa co-localized with ARs. Wall protrusions occurred co-localized with the redundant actin bundles. If these were completed in a circle, redundant septa developed. The AR is a mechanism which, in time and space, triggers cytokinesis by building a septum sequentially dependent on the AR. Aberrant septa were not capable of separating daughter cells. However, non-separated daughter cells subsequently gave rise to normal cells.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Gabriel M, Horký D, Svoboda A, Kopecká M","authors_abbrev":"Gabriel M et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Microbiology (Reading) 1998 Aug;144 ( Pt 8):2331-2344","cv_annotations":{},"doi":"10.1099/00221287-144-8-2331","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1998","pubmed_entrez_date":"1998-08-28","pubmed_publication_date":"Aug 1998","terms_by_termid":{},"title":"Cytochalasin D interferes with contractile actin ring and septum formation in Schizosaccharomyces japonicus var. versatilis.","uniquename":"PMID:9720056"}


id: PMID:29191091
data:
  {"abstract":"Coenzyme Q (CoQ) is essential for mitochondrial respiration and as a cofactor for sulfide quinone reductase. Schizosaccharomyces pombe produces a human-type CoQ 10 . Here, we analyzed CoQ in other fission yeast species. S. cryophilus and S. octosporus produce CoQ 9 . S. japonicus produces low levels of CoQ 10 , although all necessary genes for CoQ synthesis have been identified in its genome. We expressed three genes (dps1, dlp1, and ppt1) for CoQ synthesis from S. japonicus in the corresponding S. pombe mutants, and confirmed that they were functional. S. japonicus had very low levels of oxygen consumption and was essentially respiration defective, probably due to mitochondrial dysfunction. S. japonicus grows well on minimal medium during anaerobic culture, indicating that it acquires sufficient energy by fermentation. S. japonicus produces comparable levels of ethanol under both normal and elevated temperature (42 °C) conditions, at which S. pombe is not able to grow.","alleles_by_uniquename":{},"annotation_curators":[{"annotation_count":4,"community_curator":true,"file_name":null,"file_type":null,"name":"Makoto Kawamukai","orcid":null},{"annotation_count":3,"community_curator":false,"file_name":null,"file_type":null,"name":"Val Wood","orcid":"0000-0001-6330-7526"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-07-15","authors":"Kaino T, Tonoko K, Mochizuki S, Takashima Y, Kawamukai M","authors_abbrev":"Kaino T et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-09-01 07:29:31","canto_curator_name":"Makoto Kawamukai","canto_curator_role":"community","canto_first_approved_date":"2021-07-15 11:51:14","canto_session_key":"53ebb2b64b3102f9","canto_session_submitted_date":"2021-07-15 08:22:11","canto_triage_status":"Curatable","citation":"Biosci Biotechnol Biochem 2018 Jun;82(6):1031-1042","cv_annotations":{"biological_process":[{"annotations":[114133,114134],"is_not":false,"summary":null,"term":"GO:0006744"},{"annotations":[114132],"is_not":false,"summary":null,"term":"GO:0006743"}],"molecular_function":[{"annotations":[114131],"is_not":false,"summary":null,"term":"GO:0002083"},{"annotations":[114129,114130],"is_not":false,"summary":null,"term":"GO:0097269"}]},"doi":"10.1080/09168451.2017.1401914","gene_count":3,"genes_by_uniquename":{"SJAG_01865":null,"SJAG_04568":null,"SJAG_06603":null},"genetic_interactions":[[{"gene_a_uniquename":"SJAG_01865","gene_b_uniquename":"SJAG_04568","interaction_type":"Synthetic Rescue"},[{"reference_uniquename":"PMID:29191091","throughput":"low"}]]],"genotypes_by_uniquename":{},"ltp_gene_count":3,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2018","pubmed_entrez_date":"2017-12-02","pubmed_publication_date":"Jun 2018","terms_by_termid":{"GO:0002083":null,"GO:0006743":null,"GO:0006744":null,"GO:0097269":null},"title":"Schizosaccharomyces japonicus has low levels of CoQ 10  synthesis, respiration deficiency, and efficient ethanol production.","uniquename":"PMID:29191091"}


id: PMID:12795405
data:
  {"abstract":"Spectrin, a component of the membrane skeleton in erythrocytes and other animal cells, has also been identified in plant and fungal cells. However, its postulated role, i.e., the maintenance of shape and elasticity of the plasma membrane, is probably not exerted in walled cells. To study spectrin in these cells, we chose yeasts because of a high morphological variability of their life cycle. The localization of spectrin in the cells and protoplasts of Saccharomyces cerevisiae and Schizosaccharomyces japonicus var. versatilis was detected by immunoblotting, indirect immunofluorescence, and immunogold electron microscopy techniques with the use of anti-chicken and anti-human erythrocyte spectrin antibodies. A protein band of 220-240 kDa and some bands of lower relative mass were detected in cell and protoplast extracts of both yeast strains. Spectrin-like proteins were revealed by fluorescence microscopy at cell surfaces and in vacuolar membranes. Immunogold-labelling showed spectrin-like proteins in the plasma membrane, endoplasmic reticulum, vacuoles, nuclei, vesicles, mitochondria, and cell walls. The topology of spectrin was not affected by actin depolymerization with Latrunculin B nor was it changed in either act1-1 or cdc42 mutants, under restrictive conditions. Under osmotic stress, both spectrin and actin were delocalized and appeared in the form of large clusters in the cytoplasm. It is concluded that a protein cross-reacting with spectrin antibodies is present in fission and budding yeasts. Generally, it is located in the proximity of the plasma membrane and other intracellular membranes, probably as a part of the membrane skeleton. No evidence of its relationship to either actin or growth zones of the cell can be provided.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Slaninová I, Holubárová A, Svoboda A","authors_abbrev":"Slaninová I et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Can J Microbiol 2003 Mar;49(3):189-96","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2003","pubmed_entrez_date":"2003-06-11","pubmed_publication_date":"Mar 2003","terms_by_termid":{},"title":"Immunodetection of spectrin-like proteins in yeasts.","uniquename":"PMID:12795405"}


id: PMID:22641476
data:
  {"abstract":"Measuring relative genetic distances is one of the best ways to locate genetic loci. Here we report the construction of a strains set for genetic mapping in Schizosaccharomyces japonicus, which belongs to the genus Schizosaccharomyces together with the well-studied fission yeast Sz. pombe. We constructed 29 strains that bear a positive-negative selection marker at different loci. The marker was inserted every 500 kb in the genome of Sz. japonicus. Each marker thus becomes a 'scale mark' of a chromosome that behaves like a yardstick. By determining the genetic distances from the inserted markers, the relative location of a genomic mutation can be determined. We also constructed a fosmid library that covers an entire genome of Sz. japonicus. These tools together would facilitate identification and cloning of the gene.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Furuya K, Aoki K, Niki H","authors_abbrev":"Furuya K et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Yeast 2012 Jun;29(6):241-9","cv_annotations":{},"doi":"10.1002/yea.2907","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2012","pubmed_entrez_date":"2012-05-30","pubmed_publication_date":"Jun 2012","terms_by_termid":{},"title":"Construction of an insertion marker collection of Sz. japonicus (IMACS) for genetic mapping and a fosmid library covering its genome.","uniquename":"PMID:22641476"}


id: PMID:24375690
data:
  {"abstract":"The clade of Schizosaccharomyces includes 4 species: S. pombe, S. octosporus, S. cryophilus, and S. japonicus. Although all 4 species exhibit unicellular growth with a binary fission mode of cell division, S. japonicus alone is dimorphic yeast, which can transit from unicellular yeast to long filamentous hyphae. Recently it was found that the hyphal cells response to light and then synchronously activate cytokinesis of hyphae. In addition to hyphal growth, S. japonicas has many properties that aren't shared with other fission yeast. Mitosis of S. japonicas is referred to as semi-open mitosis because dynamics of nuclear membrane is an intermediate mode between open mitosis and closed mitosis. Novel genetic tools and the whole genomic sequencing of S. japonicas now provide us with an opportunity for revealing unique characters of the dimorphic yeast.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Niki H","authors_abbrev":"Niki H","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Yeast 2014 Mar;31(3):83-90","cv_annotations":{},"doi":"10.1002/yea.2996","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2014","pubmed_entrez_date":"2013-12-31","pubmed_publication_date":"Mar 2014","terms_by_termid":{},"title":"Schizosaccharomyces japonicus: the fission yeast is a fusion of yeast and hyphae.","uniquename":"PMID:24375690"}


id: PMID:32109380
data:
  {"abstract":"Eukaryotic genomes are organized within the nucleus through interactions with inner nuclear membrane (INM) proteins. How chromatin tethering to the INM is controlled in interphase and how this process contributes to subsequent mitotic nuclear envelope (NE) remodeling remains unclear. We have probed these fundamental questions using the fission yeast Schizosaccharomyces japonicus, which breaks and reforms the NE during mitosis. We show that attachments between heterochromatin and the transmembrane Lem2-Nur1 complex at the INM are remodeled in interphase by the ESCRT-III/Vps4 machinery. Failure of ESCRT-III/Vps4 to release Lem2-Nur1 from heterochromatin leads to persistent association of chromosomes with the INM throughout mitosis. At mitotic exit, such trapping of Lem2-Nur1 on heterochromatin prevents it from re-establishing nucleocytoplasmic compartmentalization. Our work identifies the Lem2-Nur1 complex as a substrate for the nuclear ESCRT machinery and explains how the dynamic tethering of chromosomes to the INM is linked to the establishment of nuclear compartmentalization.","alleles_by_uniquename":{"SJAG_01050:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01050","name":"nur1delta","uniquename":"SJAG_01050:allele-1"},"SJAG_01242:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01242","name":"vps32delta","uniquename":"SJAG_01242:allele-1"},"SJAG_01330:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01330","name":"mad2delta","uniquename":"SJAG_01330:allele-1"},"SJAG_01745:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01745","name":"lem2delta","uniquename":"SJAG_01745:allele-1"},"SJAG_03250:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03250","name":"sst4delta","uniquename":"SJAG_03250:allele-1"},"SJAG_03783:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03783","name":"vps24delta","uniquename":"SJAG_03783:allele-1"},"SJAG_03892:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_03892","name":"vps4delta","uniquename":"SJAG_03892:allele-1"},"SJAG_03892:allele-2":{"allele_type":"amino_acid_mutation","description":"E233Q","gene_uniquename":"SJAG_03892","name":"Vps4-EQ","uniquename":"SJAG_03892:allele-2"},"SJAG_03892:allele-3":{"allele_type":"amino_acid_mutation","description":"I307T L327S","gene_uniquename":"SJAG_03892","name":"vps4-ts","uniquename":"SJAG_03892:allele-3"},"SJAG_04349:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04349","name":"vps28delta","uniquename":"SJAG_04349:allele-1"},"SJAG_04489:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04489","name":"did4delta","uniquename":"SJAG_04489:allele-1"},"SJAG_04912:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_04912","name":"vps25delta","uniquename":"SJAG_04912:allele-1"},"SJAG_05207:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_05207","name":"cmp7delta","uniquename":"SJAG_05207:allele-1"}},"annotation_curators":[{"annotation_count":53,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-06-17","authors":"Pieper GH, Sprenger S, Teis D, Oliferenko S","authors_abbrev":"Pieper GH et al.","canto_added_date":"2021-05-10 02:37:07","canto_annotation_status":"APPROVED","canto_approved_date":"2021-06-17 17:46:25","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-06-17 17:46:25","canto_session_key":"89c611dbc0229af1","canto_session_submitted_date":"2021-06-17 17:46:16","canto_triage_status":"Curatable","citation":"Dev Cell 2020 04 06;53(1):27-41.e6","cv_annotations":{"cellular_component":[{"annotations":[114442],"is_not":false,"summary":null,"term":"GO:0000781"},{"annotations":[114440],"is_not":false,"summary":null,"term":"GO:0005783"},{"annotations":[114462],"is_not":false,"summary":null,"term":"GO:0000792"},{"annotations":[114467],"is_not":false,"summary":null,"term":"GO:1990343"},{"annotations":[114424],"is_not":false,"summary":null,"term":"GO:0000776"},{"annotations":[114444],"is_not":false,"summary":null,"term":"GO:0005771"},{"annotations":[114446],"is_not":false,"summary":null,"term":"GO:0032585"},{"annotations":[114445,114447],"is_not":false,"summary":null,"term":"GO:0031965"},{"annotations":[114468],"is_not":false,"summary":null,"term":"GO:0005643"},{"annotations":[114425,114430,114448],"is_not":false,"summary":null,"term":"GO:0005816"}],"molecular_function":[{"annotations":[114423],"is_not":false,"summary":null,"term":"GO:0043515"}],"multi_locus_phenotype":[{"annotations":[114453],"is_not":false,"summary":null,"term":"FYPO:0007771"},{"annotations":[114464],"is_not":false,"summary":null,"term":"FYPO:0001132"}],"single_locus_phenotype":[{"annotations":[114449,114450,114451],"is_not":false,"summary":null,"term":"FYPO:0001440"},{"annotations":[114460,114461],"is_not":false,"summary":null,"term":"FYPO:0001370"},{"annotations":[114463],"is_not":false,"summary":null,"term":"FYPO:0004718"},{"annotations":[114428,114429,114435,114436,114438,114439,114452,114454,114455,114456,114457,114458,114459],"is_not":false,"summary":null,"term":"FYPO:0007771"},{"annotations":[114441],"is_not":false,"summary":null,"term":"FYPO:0004318"},{"annotations":[114432],"is_not":false,"summary":null,"term":"FYPO:0007073"},{"annotations":[114426,114427,114433,114434],"is_not":false,"summary":null,"term":"FYPO:0007772"},{"annotations":[114437],"is_not":false,"summary":null,"term":"FYPO:0007770"},{"annotations":[114443],"is_not":false,"summary":null,"term":"FYPO:0003780"},{"annotations":[114431],"is_not":false,"summary":null,"term":"FYPO:0003657"},{"annotations":[114465,114466],"is_not":false,"summary":null,"term":"FYPO:0001234"}]},"doi":"10.1016/j.devcel.2020.01.028","gene_count":15,"genes_by_uniquename":{"SJAG_00684":null,"SJAG_01050":null,"SJAG_01242":null,"SJAG_01330":null,"SJAG_01601":null,"SJAG_01745":null,"SJAG_01777":null,"SJAG_03250":null,"SJAG_03299":null,"SJAG_03783":null,"SJAG_03892":null,"SJAG_04349":null,"SJAG_04489":null,"SJAG_04912":null,"SJAG_05207":null},"genotypes_by_uniquename":{"Vps4-EQ-E233Q-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"Vps4-EQ(E233Q aa)","display_uniquename":"Vps4-EQ-E233Q-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03892:allele-2","expression":"Not assayed or wild type"}]}]},"cmp7delta":{"display_name":"cmp7delta","display_uniquename":"cmp7delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_05207:allele-1","expression":"Null"}]}]},"cmp7delta__vps4-ts-I307T_L327S-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"cmp7delta vps4-ts(I307T L327S aa)","display_uniquename":"cmp7delta__vps4-ts-I307T_L327S-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_05207:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03892:allele-3","expression":"Not assayed or wild type"}]}]},"did4delta":{"display_name":"did4delta","display_uniquename":"did4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04489:allele-1","expression":"Null"}]}]},"lem2delta":{"display_name":"lem2delta","display_uniquename":"lem2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01745:allele-1","expression":"Null"}]}]},"mad2delta":{"display_name":"mad2delta","display_uniquename":"mad2delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01330:allele-1","expression":"Null"}]}]},"nur1delta":{"display_name":"nur1delta","display_uniquename":"nur1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01050:allele-1","expression":"Null"}]}]},"nur1delta__vps4delta":{"display_name":"nur1delta vps4delta","display_uniquename":"nur1delta__vps4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01050:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_03892:allele-1","expression":"Null"}]}]},"sst4delta":{"display_name":"sst4delta","display_uniquename":"sst4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03250:allele-1","expression":"Null"}]}]},"vps24delta":{"display_name":"vps24delta","display_uniquename":"vps24delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03783:allele-1","expression":"Null"}]}]},"vps25delta":{"display_name":"vps25delta","display_uniquename":"vps25delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04912:allele-1","expression":"Null"}]}]},"vps28delta":{"display_name":"vps28delta","display_uniquename":"vps28delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_04349:allele-1","expression":"Null"}]}]},"vps32delta":{"display_name":"vps32delta","display_uniquename":"vps32delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01242:allele-1","expression":"Null"}]}]},"vps4-ts-I307T_L327S-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"vps4-ts(I307T L327S aa)","display_uniquename":"vps4-ts-I307T_L327S-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03892:allele-3","expression":"Not assayed or wild type"}]}]},"vps4delta":{"display_name":"vps4delta","display_uniquename":"vps4delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_03892:allele-1","expression":"Null"}]}]}},"ltp_gene_count":15,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[{"evidence":"Reconstituted Complex","gene_uniquename":"SJAG_01242","interactor_uniquename":"SJAG_03892","reference_uniquename":"PMID:32109380","throughput":"low"},{"evidence":"Reconstituted Complex","gene_uniquename":"SJAG_04489","interactor_uniquename":"SJAG_03892","reference_uniquename":"PMID:32109380","throughput":"low"},{"evidence":"Reconstituted Complex","gene_uniquename":"SJAG_05207","interactor_uniquename":"SJAG_01242","reference_uniquename":"PMID:32109380","throughput":"low"},{"evidence":"Reconstituted Complex","gene_uniquename":"SJAG_05207","interactor_uniquename":"SJAG_01745","reference_uniquename":"PMID:32109380","throughput":"low"},{"evidence":"Reconstituted Complex","gene_uniquename":"SJAG_05207","interactor_uniquename":"SJAG_03892","reference_uniquename":"PMID:32109380","throughput":"low"}],"publication_year":"2020","pubmed_entrez_date":"2020-02-29","pubmed_publication_date":"06 04 2020","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000137":null,"FYPO:0001132":null,"FYPO:0001234":null,"FYPO:0001370":null,"FYPO:0001440":null,"FYPO:0003657":null,"FYPO:0003780":null,"FYPO:0004318":null,"FYPO:0004718":null,"FYPO:0007073":null,"FYPO:0007770":null,"FYPO:0007771":null,"FYPO:0007772":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"GO:0000093":null,"GO:0000776":null,"GO:0000781":null,"GO:0000792":null,"GO:0000815":null,"GO:0005643":null,"GO:0005771":null,"GO:0005783":null,"GO:0005816":null,"GO:0031965":null,"GO:0032585":null,"GO:0043515":null,"GO:1990343":null},"title":"ESCRT-III/Vps4 Controls Heterochromatin-Nuclear Envelope Attachments.","uniquename":"PMID:32109380"}


id: PMID:12402243
data:
  {"abstract":"The structure and localization of the microtubule organization centres (MTOCs) of the fission yeast Schizosaccharomyces japonicus var. japonicus were examined by fluorescence microscopy and electron microscopy. Spindle pole bodies (SPBs), which are the fungal equivalent of centrosomes, of Sz. japonicus were visualized by immunofluorescent staining using a monoclonal anti-gamma-tubulin antibody. The behaviour of the SPBs during the cell cycle mostly coincided with previous reports on the most widely used fission yeast Schizosaccharomyces pombe. We cloned the gamma-tubulin gene from Sz. japonicus by PCR using redundant sets of primers corresponding to conserved regions of known gamma-tubulins. The predicted amino acid sequence of Sz. japonicus gamma-tubulin was most similar to the Sz. pombe gamma-tubulin. Under the electron microscope, the SPBs of Sz. japonicus were detected as electron-dense multilayered structures located just outside the nuclear envelope. The SPBs of Sz. japonicus were composed of three electron-dense layers and were surrounded by fuzzy material. Each layer showed structural changes according to the progression of the cell cycle. In mitotic cells, the SPBs were located on the fenestrae of the nuclear envelopes through which the mitotic spindle microtubules ran into the nucleoplasm. Our results show that Sz. japonicus is a very potent and attractive organism for the investigation of the microtubule nucleation system and morphogenesis in yeasts. The Accession No. for the nucleotide sequence of the Sz. japonicus gtb1(+) gene is AF159163.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Horio T, Kimura N, Basaki A, Tanaka Y, Noguchi T, Akashi T, Tanaka K","authors_abbrev":"Horio T et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Yeast 2002 Nov;19(15):1335-50","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2002","pubmed_entrez_date":"2002-10-29","pubmed_publication_date":"Nov 2002","terms_by_termid":{},"title":"Molecular and structural characterization of the spindle pole bodies in the fission yeast Schizosaccharomyces japonicus var japonicus.","uniquename":"PMID:12402243"}


id: GO_REF:0000003
data:
  {"alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"canto_curator_role":"JaponicusDB","cv_annotations":{"molecular_function":[{"annotations":[67696],"is_not":false,"summary":null,"term":"GO:0003870"},{"annotations":[65303],"is_not":false,"summary":null,"term":"GO:0003986"},{"annotations":[69428],"is_not":false,"summary":null,"term":"GO:0003925"},{"annotations":[59268],"is_not":false,"summary":null,"term":"GO:0043864"},{"annotations":[66137],"is_not":false,"summary":null,"term":"GO:0052832"},{"annotations":[66138],"is_not":false,"summary":null,"term":"GO:0052833"},{"annotations":[69149],"is_not":false,"summary":null,"term":"GO:1990817"},{"annotations":[70080],"is_not":false,"summary":null,"term":"GO:0004674"},{"annotations":[60150],"is_not":false,"summary":null,"term":"GO:0003983"}]},"gene_count":8,"genes_by_uniquename":{"SJAG_00097":null,"SJAG_01885":null,"SJAG_02178":null,"SJAG_02383":null,"SJAG_02721":null,"SJAG_02985":null,"SJAG_03739":null,"SJAG_04509":null},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{"GO:0003870":null,"GO:0003925":null,"GO:0003983":null,"GO:0003986":null,"GO:0004674":null,"GO:0043864":null,"GO:0052832":null,"GO:0052833":null,"GO:1990817":null},"uniquename":"GO_REF:0000003"}


id: PMID:10379403
data:
  {"abstract":"The order Schizosaccharomycetales contains a dimorphic and two yeast species. Sch. japonicus can form both yeast cells and mycelium, depending on the substrate and the culturing conditions. Sch. pombe is a strictly unicellular organism, but it can be forced to form mycelial cell chains by inactivating members of the sep gene family. The mutations in most of the sep genes confer pleitropic phenotypes indicating functional involvement in MAP-kinase-mediated signalling pathways. Two of them were found to encode transcription factor homologues of other eukaryotes.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Sipiczki M, Grallert A, Miklós I, Zilahi E, Bozsik A, Szilágyi Z","authors_abbrev":"Sipiczki M et al.","canto_added_date":"2023-05-04 00:40:04","canto_annotation_status":"SESSION_CREATED","canto_curator_role":"JaponicusDB","canto_session_key":"eb5db4e2ead0caf4","canto_triage_status":"Cell composition or WT feature","citation":"Acta Microbiol Immunol Hung 1999;46(2-3):297-302","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1999","pubmed_entrez_date":"1999-06-24","pubmed_publication_date":"1999","terms_by_termid":{},"title":"Genetics, physiology and cytology of yeast-mycelial dimorphism in fission yeasts.","uniquename":"PMID:10379403"}


id: PMID:21873635
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  {"abstract":"The goal of the Gene Ontology (GO) project is to provide a uniform way to describe the functions of gene products from organisms across all kingdoms of life and thereby enable analysis of genomic data. Protein annotations are either based on experiments or predicted from protein sequences. Since most sequences have not been experimentally characterized, most available annotations need to be based on predictions. To make as accurate inferences as possible, the GO Consortium's Reference Genome Project is using an explicit evolutionary framework to infer annotations of proteins from a broad set of genomes from experimental annotations in a semi-automated manner. Most components in the pipeline, such as selection of sequences, building multiple sequence alignments and phylogenetic trees, retrieving experimental annotations and depositing inferred annotations, are fully automated. However, the most crucial step in our pipeline relies on software-assisted curation by an expert biologist. This curation tool, Phylogenetic Annotation and INference Tool (PAINT) helps curators to infer annotations among members of a protein family. PAINT allows curators to make precise assertions as to when functions were gained and lost during evolution and record the evidence (e.g. experimentally supported GO annotations and phylogenetic information including orthology) for those assertions. In this article, we describe how we use PAINT to infer protein function in a phylogenetic context with emphasis on its strengths, limitations and guidelines. 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id: PMID:21905090
data:
  {"abstract":"The construction of diploid cells eases genetic analysis in haploid genetic systems because diploid cells allow for the characterization of essential genes. Here, we report the construction of diploid cells using ade6 point mutants that suppress each other via interallelic complementation in the fission yeast Schizosaccharomyces japonicus var japonicus (Sz. japonicus). We constructed an ade6-domK mutant in addition to the previously described ade6-domE. Phenotypes of both mutants exhibited adenine auxotrophy and red colonies. The mutations complemented the phenotypes in a mutually dependent manner. Diploid zygotes, in which the two mutations were introduced simultaneously into the same cells, were isolated by selecting for adenine independence. Such diploid cells are apparently larger in size than haploid cells, yet have a similar nuclear/cytoplasmic ratio, and thus the nuclear size control that has been reported in Sz. pombe is also present in Sz. japonicus.","alleles_by_uniquename":{"SJAG_01081:allele-1":{"allele_type":"nonsense_mutation","description":"S427>stop","gene_uniquename":"SJAG_01081","name":"ade6-domE","uniquename":"SJAG_01081:allele-1"},"SJAG_01081:allele-2":{"allele_type":"amino_acid_mutation","description":"Q262A","gene_uniquename":"SJAG_01081","name":"ade6-domK","uniquename":"SJAG_01081:allele-2"},"SJAG_01081:allele-3":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_01081","name":"ade6delta","uniquename":"SJAG_01081:allele-3"}},"annotation_curators":[{"annotation_count":3,"community_curator":true,"file_name":null,"file_type":null,"name":"Sho Okamoto","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2022-11-23","authors":"Furuya K, Niki H","authors_abbrev":"Furuya K et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2022-11-23 13:21:47","canto_curator_name":"Sho Okamoto","canto_curator_role":"community","canto_first_approved_date":"2022-11-23 13:21:47","canto_session_key":"7c1c894d4ee8d8d3","canto_session_submitted_date":"2022-11-23 13:21:40","canto_triage_status":"Curatable","citation":"Yeast 2011 Oct;28(10):747-54","cv_annotations":{"single_locus_phenotype":[{"annotations":[114556,114557,114558],"is_not":false,"summary":null,"term":"FYPO:0000747"}]},"doi":"10.1002/yea.1898","gene_count":1,"genes_by_uniquename":{"SJAG_01081":null},"genotypes_by_uniquename":{"ade6-domE-S427>stop-nonsense_mutation-expression-not_assayed_or_wild_type":{"display_name":"ade6-domE(S427>stop)","display_uniquename":"ade6-domE-S427>stop-nonsense_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01081:allele-1","expression":"Not assayed or wild type"}]}]},"ade6-domK-Q262A-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"ade6-domK(Q262A aa)","display_uniquename":"ade6-domK-Q262A-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01081:allele-2","expression":"Not assayed or wild type"}]}]},"ade6delta":{"display_name":"ade6delta","display_uniquename":"ade6delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_01081:allele-3","expression":"Null"}]}]}},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2011","pubmed_entrez_date":"2011-09-10","pubmed_publication_date":"Oct 2011","terms_by_termid":{"FYPO:0000747":null},"title":"Construction of diploid zygotes by interallelic complementation of ade6 in Schizosaccharomyces japonicus.","uniquename":"PMID:21905090"}


id: PMID:32265131
data:
  {"abstract":"The N- and O-linked oligosaccharides from fission yeast Schizosaccharomyces pombe not only contain large amounts of d-mannose (Man) but also contain large amounts of d-galactose (Gal). Although the galactomannans of S. pombe are mainly composed of α1,2- or α1,3-linked Gals, some of the terminal α1,2-linked Gals are found to be linked to pyruvylated β1,3-linked galactose (PvGal). We have determined the structural characteristics of the N-glycans and O-glycans in three Schizosaccharomyces species (S. japonicus, S. octosporus, and S. cryophilus) using lectin blot,  1 H NMR spectroscopy, and size-fractionation high performance liquid chromatography (HPLC), and found that the galactosylation of oligosaccharides was a common feature in fission yeasts. In addition, each of the terminal Galα1,2-, Galβ1,3- and non-substituted Man residues exhibited distinct characteristics. A BLAST search of gene databases in Schizosaccharomyces identified genes homologous to pvg1 encoding pyruvyltransferase of S. pombe. These genes, when expressed in an S. pombe pvg1Δ strains, led to the pyruvylation of non-reducing terminal β-linked Gal, suggesting the biosynthetic pathway of PvGal-containing oligosaccharides is highly conserved in fission yeasts.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Fukunaga T, Tanaka N, Furumoto T, Nakakita S, Ohashi T, Higuchi Y, Maekawa H, Takegawa K","authors_abbrev":"Fukunaga T et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"J Biosci Bioeng 2020 Aug;130(2):128-136","cv_annotations":{},"doi":"10.1016/j.jbiosc.2020.03.008","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2020","pubmed_entrez_date":"2020-04-09","pubmed_publication_date":"Aug 2020","terms_by_termid":{},"title":"Characterization of N- and O-linked galactosylated oligosaccharides from fission yeast species.","uniquename":"PMID:32265131"}


id: PMID:34427722
data:
  {"abstract":"Fungal pathogens, from phytopathogenic fungus to human pathogens, are able to alternate between the yeast-like form and filamentous forms. This morphological transition (dimorphism) is in close connection with their pathogenic lifestyles and with their responses to changing environmental conditions. The mechanisms governing these morphogenetic conversions are still not fully understood. Therefore, we studied the filamentous growth of the less-known, non-pathogenic dimorphic fission yeast, S. japonicus, which belongs to an ancient and early evolved branch of the Ascomycota. Its RNA sequencing revealed that several hundred genes were up- or down-regulated in the hyphae compared to the yeast-phase cells. These genes belonged to different GO categories, confirming that mycelial growth is a rather complex process. The genes of transport- and metabolic processes appeared especially in high numbers among them. High expression of genes involved in glycolysis and ethanol production was found in the hyphae, while other results pointed to the regulatory role of the protein kinase A (PKA) pathway. The homologues of 49 S. japonicus filament-associated genes were found by sequence alignments also in seven distantly related dimorphic and filamentous species. The comparative genomic analyses between S. japonicus and the closely related but non-dimorphic S. pombe shed some light on the differences in their genomes. All these data can contribute to a better understanding of hyphal growth and those genomic rearrangements that underlie it.","alleles_by_uniquename":{},"annotation_curators":[{"annotation_count":2,"community_curator":true,"file_name":null,"file_type":null,"name":"Ida Miklos","orcid":"0000-0002-7074-4019"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-10-06","authors":"Papp LA, Ács-Szabó L, Batta G, Miklós I","authors_abbrev":"Papp LA et al.","canto_added_date":"2021-09-29 13:11:40","canto_annotation_status":"APPROVED","canto_approved_date":"2021-10-06 13:34:09","canto_curator_name":"Ida Miklos","canto_curator_role":"community","canto_first_approved_date":"2021-10-06 13:34:09","canto_session_key":"acb5c82405799ef1","canto_session_submitted_date":"2021-09-29 13:38:18","canto_triage_status":"Curatable","citation":"Curr Genet 2021 Dec;67(6):953-968","cv_annotations":{"biological_process":[{"annotations":[114137,114138],"is_not":false,"summary":null,"term":"GO:0030448"}]},"doi":"10.1007/s00294-021-01206-y","gene_count":2,"genes_by_uniquename":{"SJAG_00124":null,"SJAG_04312":null},"genotypes_by_uniquename":{},"ltp_gene_count":2,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2021","pubmed_entrez_date":"2021-08-24","pubmed_publication_date":"Dec 2021","terms_by_termid":{"GO:0030448":null},"title":"Molecular and comparative genomic analyses reveal evolutionarily conserved and unique features of the Schizosaccharomyces japonicus mycelial growth and the underlying genomic changes.","uniquename":"PMID:34427722"}


id: PMID:25318672
data:
  {"abstract":"Excess fatty acids and sterols are stored as triacylglycerols and sterol esters in specialized cellular organelles, called lipid droplets. Understanding what determines the cellular amount of neutral lipids and their packaging into lipid droplets is of fundamental and applied interest. Using two species of fission yeast, we show that cycling cells deficient in the function of the ER-resident CDP-DG synthase Cds1 exhibit markedly increased triacylglycerol content and assemble large lipid droplets closely associated with the ER membranes. We demonstrate that these unusual structures recruit the triacylglycerol synthesis machinery and grow by expansion rather than by fusion. Our results suggest that interfering with the CDP-DG route of phosphatidic acid utilization rewires cellular metabolism to adopt a triacylglycerol-rich lifestyle reliant on the Kennedy pathway. ","alleles_by_uniquename":{"SJAG_00426:allele-1":{"allele_type":"amino_acid_mutation","description":"P363S","gene_uniquename":"SJAG_00426","name":"bbl1-P363S","uniquename":"SJAG_00426:allele-1"}},"annotation_curators":[{"annotation_count":8,"community_curator":false,"file_name":null,"file_type":null,"name":"Snezhana Oliferenko","orcid":"0000-0002-8138-6851"}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-05-17","authors":"He Y, Yam C, Pomraning K, Chin JS, Yew JY, Freitag M, Oliferenko S","authors_abbrev":"He Y et al.","canto_added_date":"2021-05-10 02:38:06","canto_annotation_status":"APPROVED","canto_approved_date":"2021-05-17 12:42:41","canto_curator_name":"Snezhana Oliferenko","canto_curator_role":"JaponicusDB","canto_first_approved_date":"2021-05-17 12:42:41","canto_session_key":"f89ee2d26032c510","canto_session_submitted_date":"2021-05-17 12:42:28","canto_triage_status":"Curatable","citation":"Mol Biol Cell 2014 Dec 15;25(25):4083-95","cv_annotations":{"biological_process":[{"annotations":[114122],"is_not":false,"summary":null,"term":"GO:0016024"}],"cellular_component":[{"annotations":[114123],"is_not":false,"summary":null,"term":"GO:0005783"}],"molecular_function":[{"annotations":[114121],"is_not":false,"summary":null,"term":"GO:0004605"}],"single_locus_phenotype":[{"annotations":[114125],"is_not":false,"summary":null,"term":"FYPO:0000356"},{"annotations":[114124],"is_not":false,"summary":null,"term":"FYPO:0006433"},{"annotations":[114127],"is_not":false,"summary":null,"term":"FYPO:0004695"},{"annotations":[114126],"is_not":false,"summary":null,"term":"FYPO:0002227"},{"annotations":[114128],"is_not":false,"summary":null,"term":"FYPO:0001357"}]},"doi":"10.1091/mbc.E14-03-0832","gene_count":1,"genes_by_uniquename":{"SJAG_00426":null},"genotypes_by_uniquename":{"bbl1-P363S-P363S-amino_acid_mutation-expression-not_assayed_or_wild_type":{"display_name":"bbl1-P363S(aa)","display_uniquename":"bbl1-P363S-P363S-amino_acid_mutation-expression-not_assayed_or_wild_type","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00426:allele-1","expression":"Not assayed or wild type"}]}]}},"ltp_gene_count":1,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2014","pubmed_entrez_date":"2014-10-17","pubmed_publication_date":"15 Dec 2014","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000006":null,"FYECO:0000162":null,"FYPO:0000356":null,"FYPO:0001357":null,"FYPO:0002227":null,"FYPO:0004695":null,"FYPO:0006433":null,"FYPO_EXT:0000001":null,"GO:0004605":null,"GO:0005783":null,"GO:0008654":null,"GO:0016024":null},"title":"Increase in cellular triacylglycerol content and emergence of large ER-associated lipid droplets in the absence of CDP-DG synthase function.","uniquename":"PMID:25318672"}


id: PMID:26457121
data:
  {"abstract":"Transposable elements (TEs) are common constituents of centromeres. However, it is not known what causes this relationship. Schizosaccharomyces japonicus contains 10 families of Long Terminal Repeat (LTR)-retrotransposons and these elements cluster in centromeres and telomeres. In the related yeast, Schizosaccharomyces pombe LTR-retrotransposons Tf1 and Tf2 are distributed in the promoter regions of RNA pol II transcribed genes. Sequence analysis of TEs indicates that Tj1 of S. japonicus is related to Tf1 and Tf2, and uses the same mechanism of self-primed reverse transcription. Thus, we wondered why these related retrotransposons localized in different regions of the genome.\nTo characterize the integration behavior of Tj1 we expressed it in S. pombe. We found Tj1 was active and capable of generating de novo integration in the chromosomes of S. pombe. The expression of Tj1 is similar to Type C retroviruses in that a stop codon at the end of Gag must be present for efficient integration. 17 inserts were sequenced, 13 occurred within 12 bp upstream of tRNA genes and 3 occurred at other RNA pol III transcribed genes. The link between Tj1 integration and RNA pol III transcription is reminiscent of Ty3, an LTR-retrotransposon of Saccharomyces cerevisiae that interacts with TFIIIB and integrates upstream of tRNA genes.\nThe integration of Tj1 upstream of tRNA genes and the centromeric clustering of tRNA genes in S. japonicus demonstrate that the clustering of this TE in centromere sequences is due to a unique pattern of integration.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Guo Y, Singh PK, Levin HL","authors_abbrev":"Guo Y et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Mob DNA 2015;6:19","cv_annotations":{},"doi":"10.1186/s13100-015-0048-2","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2015","pubmed_entrez_date":"2015-10-13","pubmed_publication_date":"2015","terms_by_termid":{},"title":"A long terminal repeat retrotransposon of Schizosaccharomyces japonicus integrates upstream of RNA pol III transcribed genes.","uniquename":"PMID:26457121"}


id: PMID:22572960
data:
  {"abstract":"The aim of mitosis is to produce two daughter nuclei, each containing a chromosome complement identical to that of the mother nucleus. This can be accomplished through a variety of strategies, with \"open\" and \"closed\" modes of mitosis positioned at the opposite ends of the spectrum and a range of intermediate patterns in between. In the \"closed\" mitosis, the nuclear envelope remains intact throughout the nuclear division. In the \"open\" division type, the envelope of the original nucleus breaks down early in mitosis and reassembles around the segregated daughter genomes. In any case, the nuclear membrane has to remodel to accommodate the mitotic spindle assembly, chromosome segregation and formation of the daughter nuclei. We have recently shown that within the fission yeast clade, the mitotic control of the nuclear surface area may determine the choice between the nuclear envelope breakdown and a fully \"closed\" division. Here we discuss our data and argue that comparative cell biology studies using two fission yeast species, Schizosaccharomyces pombe and Schizosaccharomyces japonicus, could provide unprecedented insights into physiology and evolution of mitosis.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Gu Y, Yam C, Oliferenko S","authors_abbrev":"Gu Y et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Nucleus 2012 May;3(3):220-5","cv_annotations":{},"doi":"10.4161/nucl.19514","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2012","pubmed_entrez_date":"2012-05-11","pubmed_publication_date":"May 2012","terms_by_termid":{},"title":"Divergence of mitotic strategies in fission yeasts.","uniquename":"PMID:22572960"}


id: PMID:32140970
data:
  {"abstract":"In eukaryotes, chromosome ends (telomeres) are tethered to the inner nuclear membrane. During the early stages of meiosis, telomeres move along the nuclear membrane and gather near the spindle-pole body, resulting in a bouquet-like arrangement of chromosomes. This chromosomal configuration appears to be widely conserved among eukaryotes, and is assumed to play an important role in the normal progression of meiosis, by mediating the proper pairing of homologous chromosomes. In fission yeast, the Bqt1-Bqt2 protein complex plays a key role in tethering the telomere to the inner nuclear membrane. However, the structural details of the complex required to clarify how telomeres are gathered near the spindle-pole body remain enigmatic. Previously, we devised a preparation procedure for the Schizosaccharomyces japonicus Bqt1-Bqt2 complex, in which a SUMO tag was fused to the N-terminus of the Bqt1 protein. This allowed us to purify the Bqt1-Bqt2 complex from the soluble fraction. In the present study, we found that a maltose-binding protein homolog, Athe_0614, served as a better fusion partner than the SUMO protein, resulting in the marked increase in the solubility of the Bqt1-Bqt2 complex. The Athe_0614 fusion partner may open up new avenues for X-ray crystallographic analyses of the structure of the Bqt1-Bqt2 complex.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Yuzurihara H, Aizawa Y, Saotome M, Ichikawa Y, Yokoyama H, Chikashige Y, Haraguchi T, Hiraoka Y, Kurumizaka H, Kagawa W","authors_abbrev":"Yuzurihara H et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Protein J 2020 04;39(2):174-181","cv_annotations":{},"doi":"10.1007/s10930-020-09887-z","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2020","pubmed_entrez_date":"2020-03-07","pubmed_publication_date":"04 2020","terms_by_termid":{},"title":"Improved Methods for Preparing the Telomere Tethering Complex Bqt1-Bqt2 for Structural Studies.","uniquename":"PMID:32140970"}


id: PMID:8546451
data:
  {"abstract":"The phylogenesis of fungi is controversial due to their simple morphology and poor fossilization. Traditional classification supported by morphological studies and physiological traits placed the fission yeasts in one group with ascomycetous yeasts. The rRNA sequence comparisons, however, revealed an enormous evolutionary gap between Saccharomyces and Schizosaccharomyces. As shown in this review, the protein sequences also show a large gap which is almost as large as that separating Schizosaccharomyces from higher animals. Since the two yeasts share features (both cytological and molecular) in common which are also characteristic of ascomycetous fungi, their separation must have taken place later than the sequence differences may suggest. Possible reasons for the paradox are discussed. The sequence data also suggest a slower evolutionary rate in the Schizosaccharomyces lineage than in the Saccharomyces branch. In the fission yeast lineage two ramifications can be supposed. First S. japonicus (Hasegawaea japonica) branched off, then S. octosporus (Octosporomyces octosporus) separated from S. pombe.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Sipiczki M","authors_abbrev":"Sipiczki M","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Phylogeny and evolutionary studies","citation":"Antonie Van Leeuwenhoek 1995 Aug;68(2):119-49","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1995","pubmed_entrez_date":"1995-08-01","pubmed_publication_date":"Aug 1995","terms_by_termid":{},"title":"Phylogenesis of fission yeasts. Contradictions surrounding the origin of a century old genus.","uniquename":"PMID:8546451"}


id: PMID:20737410
data:
  {"abstract":"Schizosaccharomyces japonicus is a fission yeast for which new genetic tools have recently been developed. Here, we report novel plasmid vectors with high transformation efficiency and an electroporation method for Sz. japonicus. We isolated 44 replicating segments from 12 166 transformants of Sz. japonicus genomic fragments and found a chromosomal fragment, RS1, as a new replicating sequence that conferred high transformation activity to Sz. japonicus cells. This sequence was cloned into a pUC19 vector with ura4(+) of Sz. pombe (pSJU11) or the kan gene on the kanMX6 module (pSJK11) as selection markers. These plasmids transformed Sz. japonicus cells in the early-log phase by electroporation at a frequency of 123 cfu/µg for pSJK11 and 301 cfu/µg for pSJU11, which were higher than previously reported autonomously replicating sequences. Although a portion of plasmids remained in host cells by integration into the chromosome via RS1 segment, the plasmids could be recovered from transformants. The plasmid copy number was estimated to be 1.88 copies per cell by Southern blot analysis using a Sz. pombe ura4(+) probe. The plasmid containing ade6(+) suppressed the auxotrophic growth of the ade6-domE mutant, indicating that the plasmid would be useful for suppressor screening and complementation assays in Sz. japonicus. Furthermore, pSJU11 transformed Sz. pombe cells with the same frequency as the pREP2 plasmid. This study is a report to demonstrate practical use of episomal plasmid vectors for genetic research in Sz. japonicus.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Aoki K, Nakajima R, Furuya K, Niki H","authors_abbrev":"Aoki K et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Yeast 2010 Dec;27(12):1049-60","cv_annotations":{},"doi":"10.1002/yea.1815","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2010","pubmed_entrez_date":"2010-08-26","pubmed_publication_date":"Dec 2010","terms_by_termid":{},"title":"Novel episomal vectors and a highly efficient transformation procedure for the fission yeast Schizosaccharomyces japonicus.","uniquename":"PMID:20737410"}


id: PMID:31150379
data:
  {"abstract":"Quorum sensing (QS), a mechanism of microbial communication dependent on cell density, governs developmental decisions in many bacteria and in some pathogenic and non-pathogenic fungi including yeasts. In these simple eukaryotes this response is mediated by the release into the growth medium of quorum-sensing molecules (QSMs) whose concentration increases proportionally to the population density. To date the occurrence of QS is restricted to a few yeast species. We show that a QS mediated by the aromatic alcohols phenylethanol and tryptophol represses the dimorphic yeast to hypha differentiation in the fission yeast S. japonicus in response to an increased population density. In addition, the stress activated MAPK pathway (SAPK), which controls cell cycle progression and adaptation to environmental changes in this organism, constitutively represses yeast to hypha differentiation both at transcriptional and post-translational levels. Moreover, deletion of its main effectors Sty1 MAPK and Atf1 transcription factor partially suppressed the QS-dependent block of hyphal development under inducing conditions. RNAseq analysis showed that the expression of nrg1+, which encodes a putative ortholog of the transcription factor Nrg1 that represses yeast to hypha dimorphism in C. albicans, is downregulated both by QS and the SAPK pathway. Remarkably, Nrg1 may act in S. japonicus as an activator of hyphal differentiation instead of being a repressor. S. japonicus emerges as an attractive and amenable model organism to explore the QS mechanisms that regulate cellular differentiation in fungi.","alleles_by_uniquename":{"SJAG_00124:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00124","name":"SJAG_00124delta","uniquename":"SJAG_00124:allele-1"},"SJAG_00266:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_00266","name":"atf1delta","uniquename":"SJAG_00266:allele-1"},"SJAG_02013:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02013","name":"pyp1delta","uniquename":"SJAG_02013:allele-1"},"SJAG_02592:allele-1":{"allele_type":"deletion","description":"deletion","gene_uniquename":"SJAG_02592","name":"sty1delta","uniquename":"SJAG_02592:allele-1"}},"annotation_curators":[{"annotation_count":37,"community_curator":true,"file_name":null,"file_type":null,"name":"Elisa Gómez Gil","orcid":null}],"annotation_details":{},"annotation_file_curators":[],"approved_date":"2021-08-04","authors":"Gómez-Gil E, Franco A, Madrid M, Vázquez-Marín B, Gacto M, Fernández-Breis J, Vicente-Soler J, Soto T, Cansado J","authors_abbrev":"Gómez-Gil E et al.","canto_added_date":"2021-05-10 08:46:37","canto_annotation_status":"APPROVED","canto_approved_date":"2021-08-04 11:11:18","canto_curator_name":"Elisa Gómez Gil","canto_curator_role":"community","canto_first_approved_date":"2021-08-04 11:11:18","canto_session_key":"0da7a90b15f75d86","canto_session_submitted_date":"2021-08-03 17:26:10","canto_triage_status":"Curatable","citation":"PLoS Genet 2019 05;15(5):e1008192","cv_annotations":{"PSI-MOD":[{"annotations":[114342,114343,114344,114345],"is_not":false,"summary":null,"term":"MOD:00046"}],"multi_locus_phenotype":[{"annotations":[114370],"is_not":false,"summary":null,"term":"FYPO:0007779"}],"single_locus_phenotype":[{"annotations":[114338,114350],"is_not":false,"summary":null,"term":"FYPO:0004481"},{"annotations":[114366],"is_not":false,"summary":null,"term":"FYPO:0007778"},{"annotations":[114365,114368],"is_not":false,"summary":null,"term":"FYPO:0007776"},{"annotations":[114349],"is_not":false,"summary":null,"term":"FYPO:0000708"},{"annotations":[114367,114369],"is_not":false,"summary":null,"term":"FYPO:0007780"},{"annotations":[114371,114372],"is_not":false,"summary":null,"term":"FYPO:0007824"},{"annotations":[114336,114348],"is_not":false,"summary":null,"term":"FYPO:0001122"},{"annotations":[114360,114364],"is_not":false,"summary":null,"term":"FYPO:0007777"},{"annotations":[114359,114363],"is_not":false,"summary":null,"term":"FYPO:0007775"},{"annotations":[114358,114362],"is_not":false,"summary":null,"term":"FYPO:0007774"},{"annotations":[114361],"is_not":false,"summary":null,"term":"FYPO:0007779"},{"annotations":[114341,114353],"is_not":false,"summary":null,"term":"FYPO:0000097"},{"annotations":[114340,114352],"is_not":false,"summary":null,"term":"FYPO:0000726"},{"annotations":[114339,114351],"is_not":false,"summary":null,"term":"FYPO:0000271"},{"annotations":[114354],"is_not":false,"summary":null,"term":"FYPO:0000841"},{"annotations":[114337],"is_not":false,"summary":null,"term":"FYPO:0000280"},{"annotations":[114357],"is_not":false,"summary":null,"term":"FYPO:0000648"}]},"doi":"10.1371/journal.pgen.1008192","gene_count":4,"genes_by_uniquename":{"SJAG_00124":null,"SJAG_00266":null,"SJAG_02013":null,"SJAG_02592":null},"genotypes_by_uniquename":{"SJAG_00124delta":{"display_name":"SJAG_00124delta","display_uniquename":"SJAG_00124delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00124:allele-1","expression":"Null"}]}]},"SJAG_00124delta__sty1delta":{"display_name":"SJAG_00124delta sty1delta","display_uniquename":"SJAG_00124delta__sty1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00124:allele-1","expression":"Null"}]},{"expressed_alleles":[{"allele_uniquename":"SJAG_02592:allele-1","expression":"Null"}]}]},"atf1delta":{"display_name":"atf1delta","display_uniquename":"atf1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_00266:allele-1","expression":"Null"}]}]},"pyp1delta":{"display_name":"pyp1delta","display_uniquename":"pyp1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02013:allele-1","expression":"Null"}]}]},"sty1delta":{"display_name":"sty1delta","display_uniquename":"sty1delta","loci":[{"expressed_alleles":[{"allele_uniquename":"SJAG_02592:allele-1","expression":"Null"}]}]}},"ltp_gene_count":4,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2019","pubmed_entrez_date":"2019-06-01","pubmed_publication_date":"05 2019","terms_by_termid":{"FYECO:0000004":null,"FYECO:0000078":null,"FYECO:0000137":null,"FYECO:0000207":null,"FYECO:0000272":null,"FYECO:0000314":null,"FYPO:0000097":null,"FYPO:0000271":null,"FYPO:0000280":null,"FYPO:0000648":null,"FYPO:0000708":null,"FYPO:0000726":null,"FYPO:0000841":null,"FYPO:0001122":null,"FYPO:0004481":null,"FYPO:0007774":null,"FYPO:0007775":null,"FYPO:0007776":null,"FYPO:0007777":null,"FYPO:0007778":null,"FYPO:0007779":null,"FYPO:0007780":null,"FYPO:0007824":null,"FYPO_EXT:0000001":null,"FYPO_EXT:0000002":null,"FYPO_EXT:0000003":null,"GO:0034599":null,"GO:0034605":null,"GO:0071475":null,"GO:1904547":null,"MOD:00046":null},"title":"Quorum sensing and stress-activated MAPK signaling repress yeast to hypha transition in the fission yeast Schizosaccharomyces japonicus.","uniquename":"PMID:31150379"}


id: PMID:7166567
data:
  {"abstract":"The fine structure of ascospore formation in the fission yeasts Schizosaccharomyces pombe and Schizosaccharomyces japonicus var. japonicus was studied by serial thin-sectioning and electron microscopy. The morphogenetic events were almost the same in both species. Ascospore development was initiated by the formation of the forespore membrane on the cytoplasmic side of the differentiated nucleus-associated organelle (NAO) in the interval between meiosis I and II in S. pombe, or during the post-meiotic nuclear division in S. japonicus, and the process proceeded almost synchronously through the two or four nuclei in the ascus. The forespore membrane developed by fusion of the cytoplasmic vesicles and this was clearly demonstrated in S. japonicus where the behaviour of vesicles involved in the forespore membrane development could be traced as they were marked by the presence of electron-dense granules. The staining technique, by phosphotungustic acid--chromic acid (PTA-CA) after treatment with periodic acid, was used to attempt to elucidate the origin and the nature of the forespore membrane. The method specific to plasmalemma-type membranes stained both ascus and ascospore plasmalemmas; the forespore membrane was not stained at first but developed the same affinity for stain as the plasma membrane in the course of ascospore development. The results suggest that the forespore membrane did not come directly from the ascus plasma membrane, but from another membrane system such as the endoplasmic reticulum. Spore wall material was deposited in the space between the inner and outer leaflets of the forespore membrane.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Tanaka K, Hirata A","authors_abbrev":"Tanaka K et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"J Cell Sci 1982 Aug;56:263-79","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"1982","pubmed_entrez_date":"1982-08-01","pubmed_publication_date":"Aug 1982","terms_by_termid":{},"title":"Ascospore development in the fission yeasts Schizosaccharomyces pombe and S. japonicus.","uniquename":"PMID:7166567"}


id: PMID:28342076
data:
  {"abstract":"Environmental glucose is an important regulator of biological processes, as it can launch different cell processes depending on its concentration. Thus, low glucose concentration can induce entry into quiescence, which ensures long-term viability for the cells or in other cases mycelial growth in the dimorphic species, which, in turn, provides the cells with fresh nutrients. Several genes, such as the genes of cAMP cascade, are involved in glucose sensing and response. Since this signal transduction pathway seemed to be an evolutionarily conserved process, we assumed that its genes were also conserved and preserved their functional homology. To obtain evidence, Schizosaccharomyces pombe rsv1 and its orthologous genes were investigated using in silico and experimental approaches. Our results supported that the Rsv1 zinc-finger transcription factors of Schizosaccharomyces japonicus and Schizosaccharomyces octosporus and the Candida albicans cas5p were really functional homologues of the S. pombe Rsv1. Namely, the homologous proteins were able to restore mutant phenotype of the S. pombe rsv1-deleted cells. Bioinformatic anaysis revealed that the most conserved parts of the proteins always contained the C2H2 domains and the complementation abilities of the counterpart genes were not uniform regarding the investigated features, which can be in connection with the conserved regions outside C2H2.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Pataki E, Sipiczki M, Miklos I","authors_abbrev":"Pataki E et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Sequence feature or region","citation":"Curr Microbiol 2017 Jun;74(6):710-717","cv_annotations":{},"doi":"10.1007/s00284-017-1227-9","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2017","pubmed_entrez_date":"2017-03-26","pubmed_publication_date":"Jun 2017","terms_by_termid":{},"title":"Schizosaccharomyces pombe rsv1 Transcription Factor and its Putative Homologues Preserved their Functional Homology and are Evolutionarily Conserved.","uniquename":"PMID:28342076"}


id: PMID:26263485
data:
  {"abstract":"Cytokinesis must be regulated in time and space in order to preserve genome integrity during cell proliferation and to allow daughter cells to adopt distinct fates and geometries during differentiation. The fission yeast Schizosaccharomyces pombe has been a popular model organism for understanding spatiotemporal regulation of cytokinesis in a symmetrically dividing cell. Recent work on another member of the same genus, Schisozaccharomyces japonicus, suggests that S. pombe may have evolved an unusual division site placement mechanism based on a recently duplicated anillin paralog. Here we discuss an extraordinary evolutionary plasticity of cytokinesis within the fission yeast clade and argue that the comparative cell biology approach may provide functional insights beyond those afforded by scrutinizing individual model species.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Gu Y, Oliferenko S","authors_abbrev":"Gu Y et al.","canto_added_date":"2023-05-04 00:40:04","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Curr Opin Microbiol 2015 Dec;28:18-25","cv_annotations":{},"doi":"10.1016/j.mib.2015.07.011","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2015","pubmed_entrez_date":"2015-08-12","pubmed_publication_date":"Dec 2015","terms_by_termid":{},"title":"Comparative biology of cell division in the fission yeast clade.","uniquename":"PMID:26263485"}


id: PMID:26104357
data:
  {"abstract":"Cells of the highly diverged Schizosaccharomyces (S.) pombe and S. japonicus fission yeasts exist in one of two sex/mating types, called P (for plus) or M (for minus), specified by which allele, M or P, resides at mat1. The fission yeasts have evolved an elegant mechanism for switching P or M information at mat1 by a programmed DNA recombination event with a copy of one of the two silent mating-type genes residing nearby in the genome. The switching process is highly cell-cycle and generation dependent such that only one of four grandchildren of a cell switches mating type. Extensive studies of fission yeast established the natural DNA strand chirality at the mat1 locus as the primary basis of asymmetric cell division. The asymmetry results from a unique site- and strand-specific epigenetic \"imprint\" at mat1 installed in one of the two chromatids during DNA replication. The imprint is inherited by one daughter cell, maintained for one cell cycle, and is then used for initiating recombination during mat1 replication in the following cell cycle. This mechanism of cell-type switching is considered to be unique to these two organisms, but determining the operation of such a mechanism in other organisms has not been possible for technical reasons. This review summarizes recent exciting developments in the understanding of mating-type switching in fission yeasts and extends these observations to suggest how such a DNA strand-based epigenetic mechanism of cellular differentiation could also operate in diploid organisms. ","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Klar AJS, Ishikawa K, Moore S","authors_abbrev":"Klar AJS et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Review or comment","citation":"Microbiol Spectr 2014 Oct;2(5)","cv_annotations":{},"doi":"10.1128/microbiolspec.MDNA3-0003-2014","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2014","pubmed_entrez_date":"2015-06-25","pubmed_publication_date":"Oct 2014","terms_by_termid":{},"title":"A Unique DNA Recombination Mechanism of the Mating/Cell-type Switching of Fission Yeasts: a Review.","uniquename":"PMID:26104357"}


id: GO_REF:0000041
data:
  {"alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"canto_curator_role":"JaponicusDB","cv_annotations":{"biological_process":[{"annotations":[66140],"is_not":false,"summary":null,"term":"GO:0006021"},{"annotations":[67700],"is_not":false,"summary":null,"term":"GO:0006782"}]},"gene_count":2,"genes_by_uniquename":{"SJAG_00097":null,"SJAG_03739":null},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{"GO:0006021":null,"GO:0006782":null},"uniquename":"GO_REF:0000041"}


id: GO_REF:0000043
data:
  {"alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"canto_curator_role":"JaponicusDB","cv_annotations":{"biological_process":[{"annotations":[67931],"is_not":false,"summary":null,"term":"GO:0009088"}],"molecular_function":[{"annotations":[66092,66800],"is_not":false,"summary":null,"term":"GO:0003779"},{"annotations":[69808],"is_not":false,"summary":null,"term":"GO:0004812"},{"annotations":[60089],"is_not":false,"summary":null,"term":"GO:0004190"},{"annotations":[57107,57633,64484,66546],"is_not":false,"summary":null,"term":"GO:0005524"},{"annotations":[67515],"is_not":false,"summary":null,"term":"GO:0008061"},{"annotations":[57973,67619],"is_not":false,"summary":null,"term":"GO:0008483"}]},"gene_count":12,"genes_by_uniquename":{"SJAG_00152":null,"SJAG_00521":null,"SJAG_00620":null,"SJAG_00691":null,"SJAG_01595":null,"SJAG_01874":null,"SJAG_01953":null,"SJAG_02263":null,"SJAG_02860":null,"SJAG_03420":null,"SJAG_03692":null,"SJAG_03856":null},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"terms_by_termid":{"GO:0003779":null,"GO:0004190":null,"GO:0004812":null,"GO:0005524":null,"GO:0008061":null,"GO:0008483":null,"GO:0009088":null},"uniquename":"GO_REF:0000043"}


id: PMID:23150598
data:
  {"abstract":"A key question in developmental biology addresses the mechanism of asymmetric cell division. Asymmetry is crucial for generating cellular diversity required for development in multicellular organisms. As one of the potential mechanisms, chromosomally borne epigenetic difference between sister cells that changes mating/cell type has been demonstrated only in the Schizosaccharomyces pombe fission yeast. For technical reasons, it is nearly impossible to determine the existence of such a mechanism operating during embryonic development of multicellular organisms. Our work addresses whether such an epigenetic mechanism causes asymmetric cell division in the recently sequenced fission yeast, S. japonicus (with 36% GC content), which is highly diverged from the well-studied S. pombe species (with 44% GC content). We find that the genomic location and DNA sequences of the mating-type loci of S. japonicus differ vastly from those of the S. pombe species. Remarkably however, similar to S. pombe, the S. japonicus cells switch cell/mating type after undergoing two consecutive cycles of asymmetric cell divisions: only one among four \"granddaughter\" cells switches. The DNA-strand-specific epigenetic imprint at the mating-type locus1 initiates the recombination event, which is required for cellular differentiation. Therefore the S. pombe and S. japonicus mating systems provide the first two examples in which the intrinsic chirality of double helical structure of DNA forms the primary determinant of asymmetric cell division. Our results show that this unique strand-specific imprinting/segregation epigenetic mechanism for asymmetric cell division is evolutionary conserved. Motivated by these findings, we speculate that DNA-strand-specific epigenetic mechanisms might have evolved to dictate asymmetric cell division in diploid, higher eukaryotes as well.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Yu C, Bonaduce MJ, Klar AJ","authors_abbrev":"Yu C et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"Genetics 2013 Jan;193(1):85-94","cv_annotations":{},"doi":"10.1534/genetics.112.146233","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2013","pubmed_entrez_date":"2012-11-15","pubmed_publication_date":"Jan 2013","terms_by_termid":{},"title":"Defining the epigenetic mechanism of asymmetric cell division of Schizosaccharomyces japonicus yeast.","uniquename":"PMID:23150598"}


id: PMID:33022982
data:
  {"abstract":"Nowadays commercial preparations of yeast polysaccharides (PSs), in particular mannoproteins, are widely used for wine colloidal and tartrate salt stabilization. In this context, the industry has developed different processes for the isolation and purification of PSs from the cell wall of  Saccharomyces cerevisiae . This yeast releases limited amounts of mannoproteins in the growth medium, thus making their direct isolation from the culture broth not economically feasible. On the contrary,  Schizosaccharomyces japonicus , a non- Saccharomyces  yeast isolated from wine, releases significant amounts of PSs during the alcoholic fermentation. In the present work, PSs released by  Sch. japonicus  were recovered from the growth medium by ultrafiltration and their impact on the wine colloidal stability was evaluated. Interestingly, these PSs contribute positively to the wine protein stability. The visible haziness of the heat-treated wine decreases as the concentration of added PSs increases. SDS-PAGE Gel electrophoresis results of the haze and of the supernatant after the heat stability test are consistent with the turbidity measurements. Moreover, particle size distributions of the heat-treated wines, as obtained by Dynamic Light Scattering (DLS), show a reduction in the average dimension of the protein aggregates as the concentration of added PSs increases.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Millarini V, Ignesti S, Cappelli S, Ferraro G, Adessi A, Zanoni B, Fratini E, Domizio P","authors_abbrev":"Millarini V et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Biotech","citation":"Foods 2020 Oct 03;9(10)","cv_annotations":{},"doi":"10.3390/foods9101407","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2020","pubmed_entrez_date":"2020-10-07","pubmed_publication_date":"03 Oct 2020","terms_by_termid":{},"title":"Protection of Wine from Protein Haze Using  Schizosaccharomyces japonicus  Polysaccharides.","uniquename":"PMID:33022982"}


id: PMID:11921097
data:
  {"abstract":"The dimorphic fission yeast Schizosaccharomyces japonicus has proved to be an excellent experimental model for the investigation of the eukaryotic cell. Here we show that it has a haplontic life cycle, in which the diploid phase is confined to the zygote. To make it amenable to genetic and molecular analysis, we generated genetic markers and cloned a genomic sequence which acts as ars when integrated into a plasmid. Diploids suitable for testing complementation and recombination between markers can be formed by protoplast fusion. The complementation tests and the recombination frequencies determined in octads of spores identified 28 non-allelic groups (genes) of mutations of the auxotrophic and mycelium-negative mutants. Two groups of linked markers were also identified. The cloned fragment, which expresses ars activity, encodes a putative amino acid sequence highly similar to a conserved domain of proteins Cut1 (Schizosaccharomyces pombe), BimB (Aspergillus nidulans) and Esp1 (Saccharomyces cerevisiae).","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Bozsik A, Szilagyi Z, Benko Z, Sipiczki M","authors_abbrev":"Bozsik A et al.","canto_added_date":"2021-05-10 08:46:37","canto_curator_role":"JaponicusDB","canto_triage_status":"Method or reagent","citation":"Yeast 2002 Apr;19(6):485-98","cv_annotations":{},"gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2002","pubmed_entrez_date":"2002-03-29","pubmed_publication_date":"Apr 2002","terms_by_termid":{},"title":"Marker construction and cloning of a cut1-like sequence with ARS activity in the fission yeast Schizosaccharomyces japonicus.","uniquename":"PMID:11921097"}


id: PMID:37088673
data:
  {"abstract":"Making wine via spontaneous fermentation without sulfur dioxide and commercial yeast (spontaneous winemaking) is increasing in recent year, but there is scant research regarding microbial communities present in Japan during spontaneous winemaking using culture-independent molecular methods. We analyzed fungal communities and populations during laboratory-scale spontaneous winemaking using sterilized labware to avoid winery-resident microbes. In the spontaneous fermentation of four grape varieties (Pinot Noir, Riesling, Koshu, and Koshusanjaku) grown in the same Japanese vineyard, our analysis of yeast and other fungal species by next-generation sequencing based on the ITS1 region demonstrated that Saccharomyces cerevisiae was eventually dominant in seven of 12 fermentation batches (three replications for each grape variety), whereas non-Saccharomyces species (e.g., Schizosaccharomyces japonicus, Lachancea dasiensis, and Hanseniaspora valbyensis) became dominant in four batches at the end of fermentation. In another batch, lactic acid bacteria (LAB) became dominant and the fermentation remained incomplete. Diverse microbes were involved in the spontaneous fermentation (particularly in Koshusanjaku), indicating that residual sugar remained and lactic and acetic acid largely increased. Compared to the control wine made with SO 2  and commercial yeast, the concentration of lactic acid was 47-fold higher in the must dominated by L. dasiensis, and the concentrations of acetic acid and lactic acid were 10-fold and 20-fold higher in the must dominated by LAB, respectively. Even when indigenous S. cerevisiae became dominant, the finished wines obtained high sensory-analysis scores for complexity but low scores for varietal typicality, indicating the risk of fermentation with unselected wild yeast on the grapes grown in Japan.","alleles_by_uniquename":{},"annotation_curators":[],"annotation_details":{},"annotation_file_curators":[],"authors":"Shimizu H, Kamada A, Koyama K, Iwashita K, Goto-Yamamoto N","authors_abbrev":"Shimizu H et al.","canto_added_date":"2023-05-04 00:40:03","canto_curator_role":"JaponicusDB","canto_triage_status":"Cell composition or WT feature","citation":"J Biosci Bioeng 2023 Apr 21;","cv_annotations":{},"doi":"10.1016/j.jbiosc.2023.03.013","gene_count":0,"genes_by_uniquename":{},"genotypes_by_uniquename":{},"ltp_gene_count":0,"ortholog_annotations":[],"paralog_annotations":[],"physical_interactions":[],"publication_year":"2023","pubmed_entrez_date":"2023-04-23","pubmed_publication_date":"21 Apr 2023","terms_by_termid":{},"title":"Yeast diversity during the spontaneous fermentation of wine with only the microbiota on grapes cultivated in Japan.","uniquename":"PMID:37088673"}


